WordNet

of or relating to a focus; "focal length"
having or localized centrally at a focus; "focal point"; "focal infection"
a fibrous band of scar tissue that binds together normally separate anatomical structures
abnormal union of bodily tissues; most common in the abdomen
an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
the basic unit of money in Papua New Guinea

PrepTutorEJDIC

焦点の
粘着,付着

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/03/09 14:45:49」(JST)

wiki en

PTK2 protein tyrosine kinase 2 (PTK2), also known as Focal Adhesion Kinase (FAK), is a protein that, in humans, is encoded by the PTK2 gene.^[2] PTK2 is a focal adhesion-associated protein kinase involved in cellular adhesion (how cells stick to each other and their surroundings) and spreading processes (how cells move around).^[3] It has been shown that when FAK was blocked, breast cancer cells became less metastastic due to decreased mobility.^[4]

Function

This gene encodes a cytosolic protein tyrosine kinase that is found concentrated in the focal adhesions that form among cells attaching to extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases that included PYK2 but lacks significant sequence similarity to kinases from other subfamilies. With the exception of certain types of blood cells, most cells express FAK. FAK tyrosine kinase activity can be activated, which plays a key important early step in cell migration. FAK activity elicits intracellular signal transduction pathways that promote the turn-over of cell contacts with the extracellular matrix, promoting cell migration. FAK is required during development, with loss of FAK resulting in lethality. It seems to be a paradox that FAK is not absolutely required for cell migration, and may play other roles in the cell, including the regulation of the tumor suppressor p53. At least four transcript variants encoding four different isoforms have been found for this gene, but the full-length natures of only two of them have been determined.^[5]

FAK is a protein of 125 kD recruited as a participant in focal adhesion dynamics between cells, and has a role in motility and cell survival. FAK is a highly conserved, non-receptor tyrosine kinase originally identified as a substrate for the oncogene protein tyrosine kinase v-src.^[6] This cytosolic kinase has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival. FAK is typically located at structures known as focal adhesions, these are multi-protein structures that link the extracellular matrix (ECM) to the cytoplasmic cytoskeleton. Additional components of focal adhesions include actin, filamin, vinculin, talin, paxillin and tensin.^[7]

Regulation

FAK is phosphorylated in response to integrin engagement, growth factor stimulation, and the action of mitogenic neuropeptides.^[8]^[9] Integrin receptors are heterodimeric transmembrane glycoproteins that cluster upon ECM engagement leading to FAK phosphorylation and recruitment to focal adhesions.^[10]^[11]

Structure

Focal adhesion kinase has a number of defined regions.

C-terminus

A carboxy-terminal region of one hundred and fifty-nine amino acids, the focal adhesion targeting domain (FAT), has been shown to be responsible for targeting FAK to focal adhesions.^[12] Paxillin, a focal adhesion adaptor protein binds to FAK at a carboxy-terminal domain that overlaps the FAT domain.^[13]

N-terminus

The function of the amino-terminal domain is less clear, but it has been shown to interact with the beta-1 integrin subunit in vitro and is thought to be involved in the transduction of signals from ECM-integrin clusters.^[14] However, a recent study has called into question the importance of this interaction and suggested that interaction with the cytoplasmic region of the beta-3 integrin subunit is important.^[15]

The amino-terminal domains of FAK share a significant sequence similarity with the band 4.1 domain first identified in erythrocytes. This 4.1 band domain binds to the cytoplasmic region of transmembrane proteins including glycophorin C, actin and spectrin.^[16] This suggests that the amino-terminal region of FAK may have a role in anchoring the cytoskeleton, the exact nature of this role has not been clarified as yet.

Catalytic/Regulatory Domain

Between the amino and the carboxy regions lies the catalytic domain. Phosphorylation of the activation loop within this kinase domain is important for the kinase activity of FAK.^[17]

Interactions

PTK2 has been shown to interact with TSC2,^[18] NCK1,^[19]^[20] Janus kinase 2,^[21]^[22] TLN1,^[23]^[24] TGFB1I1,^[25]^[26]^[27] BCAR1,^[28]^[29]^[30]^[31]^[32]^[33] Deleted in Colorectal Cancer,^[34] PIK3R1,^[35] NEDD9,^[36] Paxillin,^[24]^[25]^[33]^[37]^[38]^[39]^[40]^[41]^[42]^[43] CRK,^[29]^[44] Integrin, beta 5,^[45] GIT1,^[46]^[47]^[48] CD61,^[45]^[49] STAT1,^[50] PTEN,^[51]^[52] Src,^[29]^[44]^[53]^[54]^[55]^[56] BMX,^[57] Grb2,^[30]^[44]^[55]^[58]^[59] GRB7,^[60] RB1CC1,^[61] Syk,^[49]^[62] FYN,^[55]^[63] NEO1,^[34] P53,^[64] MAPK8IP3,^[65] IRS1^[56] and NCK2.^[20]

References

^ PMID 12005431 (PubMed)
Citation will be completed automatically in a few minutes. Jump the queue or expand by hand
^ André E, Becker-André M (January 1993). "Expression of an N-terminally truncated form of human focal adhesion kinase in brain". Biochemical and biophysical research communications 190 (1): 140–7. doi:10.1006/bbrc.1993.1022. PMID 8422239.
^ Blackshaw, S. E.; Dow, J. Kamal; Lackie, J. M. (1999). The dictionary of cell and molecular biology (3rd ed.). San Diego: Academic Press. ISBN 0-12-432565-3.
^ Physorg:When cancer cells can't let go
^ "Entrez Gene: PTK2 PTK2 protein tyrosine kinase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5747.
^ Guan JL, Shalloway D (August 1992). "Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation". Nature 358 (6388): 690–2. doi:10.1038/358690a0. PMID 1379699.
^ Chrzanowska-Wodnicka M, Burridge K (June 1996). "Rho-stimulated contractility drives the formation of stress fibers and focal adhesions". The Journal of cell biology 133 (6): 1403–15. doi:10.1083/jcb.133.6.1403. PMC 2120895. PMID 8682874. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120895.
^ Abedi H, Zachary I (June 1997). "Vascular endothelial growth factor stimulates tyrosine phosphorylation and recruitment to new focal adhesions of focal adhesion kinase and paxillin in endothelial cells". The Journal of biological chemistry 272 (24): 15442–51. doi:10.1074/jbc.272.24.15442. PMID 9182576.
^ Zachary I, Rozengurt E (December 1992). "Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes". Cell 71 (6): 891–4. doi:10.1016/0092-8674(92)90385-P. PMID 1458538.
^ Burridge K, Fath K, Kelly T, Nuckolls G, Turner C (1988). "Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton". Annual review of cell biology 4: 487–525. doi:10.1146/annurev.cb.04.110188.002415. PMID 3058164.
^ Burridge K, Turner CE, Romer LH (November 1992). "Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly". The Journal of cell biology 119 (4): 893–903. doi:10.1083/jcb.119.4.893. PMC 2289706. PMID 1385444. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289706.
^ Hildebrand JD, Schaller MD, Parsons JT (November 1993). "Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions". The Journal of cell biology 123 (4): 993–1005. doi:10.1083/jcb.123.4.993. PMC 2200138. PMID 8227154. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2200138.
^ Hildebrand JD, Schaller MD, Parsons JT (1 June 1995). "Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase". Molecular biology of the cell 6 (6): 637–47. PMC 301225. PMID 7579684. http://www.molbiolcell.org/cgi/content/abstract/6/6/637.
^ Schaller MD, Otey CA, Hildebrand JD, Parsons JT (September 1995). "Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains". The Journal of cell biology 130 (5): 1181–7. doi:10.1083/jcb.130.5.1181. PMC 2120552. PMID 7657702. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120552.
^ Tahiliani PD, Singh L, Auer KL, LaFlamme SE (March 1997). "The role of conserved amino acid motifs within the integrin beta3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation". The Journal of biological chemistry 272 (12): 7892–8. doi:10.1074/jbc.272.12.7892. PMID 9065456.
^ Girault JA, Labesse G, Mornon JP, Callebaut I (December 1998). "Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction". Molecular medicine (Cambridge, Mass.) 4 (12): 751–69. PMC 2230389. PMID 9990861. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2230389.
^ Calalb MB, Polte TR, Hanks SK (1 February 1995). "Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases". Molecular and cellular biology 15 (2): 954–63. PMC 231984. PMID 7529876. http://mcb.asm.org/cgi/content/abstract/15/2/954.
^ Gan, Boyi; Yoo Youngdong, Guan Jun-Lin (Dec. 2006). "Association of focal adhesion kinase with tuberous sclerosis complex 2 in the regulation of s6 kinase activation and cell growth". J. Biol. Chem. (United States) 281 (49): 37321–9. doi:10.1074/jbc.M605241200. ISSN 0021-9258. PMID 17043358.
^ Minegishi, M; Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (Oct. 1996). "Structure and function of Cas-L, a 105-kD Crk-associated substrate- related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes". J. Exp. Med. (UNITED STATES) 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. ISSN 0022-1007. PMC 2192828. PMID 8879209. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2192828.
^ ^a ^b Goicoechea, Silvia M; Tu Yizeng, Hua Yun, Chen Ka, Shen Tang-Long, Guan Jun-Lin, Wu Chuanyue (Jul. 2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". Int. J. Biochem. Cell Biol. (England) 34 (7): 791–805. doi:10.1016/S1357-2725(02)00002-X. ISSN 1357-2725. PMID 11950595.
^ Zhu, T; Goh E L, Lobie P E (Apr. 1998). "Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription". J. Biol. Chem. (UNITED STATES) 273 (17): 10682–9. doi:10.1074/jbc.273.17.10682. ISSN 0021-9258. PMID 9553131.
^ Ryu, H; Lee J H, Kim K S, Jeong S M, Kim P H, Chung H T (Aug. 2000). "Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin". J. Immunol. (UNITED STATES) 165 (4): 2116–23. ISSN 0022-1767. PMID 10925297.
^ Chen, H C; Appeddu P A, Parsons J T, Hildebrand J D, Schaller M D, Guan J L (Jul. 1995). "Interaction of focal adhesion kinase with cytoskeletal protein talin". J. Biol. Chem. (UNITED STATES) 270 (28): 16995–9. doi:10.1074/jbc.270.28.16995. ISSN 0021-9258. PMID 7622520.
^ ^a ^b Zheng, C; Xing Z, Bian Z C, Guo C, Akbay A, Warner L, Guan J L (Jan. 1998). "Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion". J. Biol. Chem. (UNITED STATES) 273 (4): 2384–9. doi:10.1074/jbc.273.4.2384. ISSN 0021-9258. PMID 9442086.
^ ^a ^b Matsuya, M; Sasaki H, Aoto H, Mitaka T, Nagura K, Ohba T, Ishino M, Takahashi S, Suzuki R, Sasaki T (Jan. 1998). "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". J. Biol. Chem. (UNITED STATES) 273 (2): 1003–14. doi:10.1074/jbc.273.2.1003. ISSN 0021-9258. PMID 9422762.
^ Nishiya, N; Tachibana K, Shibanuma M, Mashimo J I, Nose K (Aug. 2001). "Hic-5-Reduced Cell Spreading on Fibronectin: Competitive Effects between Paxillin and Hic-5 through Interaction with Focal Adhesion Kinase". Mol. Cell. Biol. (United States) 21 (16): 5332–45. doi:10.1128/MCB.21.16.5332-5345.2001. ISSN 0270-7306. PMC 87257. PMID 11463817. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=87257.
^ Thomas, S M; Hagel M, Turner C E (Jan. 1999). "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". J. Cell. Sci. (ENGLAND) 112 (2): 181–90. ISSN 0021-9533. PMID 9858471.
^ Salgia, R; Pisick E, Sattler M, Li J L, Uemura N, Wong W K, Burky S A, Hirai H, Chen L B, Griffin J D (Oct. 1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". J. Biol. Chem. (UNITED STATES) 271 (41): 25198–203. doi:10.1074/jbc.271.41.25198. ISSN 0021-9258. PMID 8810278.
^ ^a ^b ^c Hsia, Datsun A; Mitra Satyajit K, Hauck Christof R, Streblow Daniel N, Nelson Jay A, Ilic Dusko, Huang Shuang, Li Erguang, Nemerow Glen R, Leng Jay, Spencer Kathryn S R, Cheresh David A, Schlaepfer David D (Mar. 2003). "Differential regulation of cell motility and invasion by FAK". J. Cell Biol. (United States) 160 (5): 753–67. doi:10.1083/jcb.200212114. ISSN 0021-9525. PMC 2173366. PMID 12615911. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173366.
^ ^a ^b Hildebrand, J D; Taylor J M, Parsons J T (Jun. 1996). "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase". Mol. Cell. Biol. (UNITED STATES) 16 (6): 3169–78. ISSN 0270-7306. PMC 231310. PMID 8649427. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231310.
^ Chellaiah, M A; Biswas R S, Yuen D, Alvarez U M, Hruska K A (Dec. 2001). "Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin". J. Biol. Chem. (United States) 276 (50): 47434–44. doi:10.1074/jbc.M107494200. ISSN 0021-9258. PMID 11577104.
^ Okabe, Seiichi; Fukuda Seiji, Broxmeyer Hal E (Jul. 2002). "Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in a T-lymphocyte line". Exp. Hematol. (Netherlands) 30 (7): 761–6. doi:10.1016/S0301-472X(02)00823-8. ISSN 0301-472X. PMID 12135674.
^ ^a ^b Wang, J F; Park I W, Groopman J E (Apr. 2000). "Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood (UNITED STATES) 95 (8): 2505–13. ISSN 0006-4971. PMID 10753828.
^ ^a ^b Ren, Xiu-Rong; Ming Guo-Li, Xie Yi, Hong Yan, Sun Dong-Mei, Zhao Zhong-Qiu, Feng Zhu, Wang Qiang, Shim Sangwoo, Chen Zhou-Feng, Song Hong-Jun, Mei Lin, Xiong Wen-Cheng (Nov. 2004). "Focal adhesion kinase in netrin-1 signaling". Nat. Neurosci. (United States) 7 (11): 1204–12. doi:10.1038/nn1330. ISSN 1097-6256. PMID 15494733.
^ Guinebault, C; Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H (May. 1995). "Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase". J. Cell Biol. (UNITED STATES) 129 (3): 831–42. doi:10.1083/jcb.129.3.831. ISSN 0021-9525. PMC 2120444. PMID 7537275. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120444.
^ Law, S F; Estojak J, Wang B, Mysliwiec T, Kruh G, Golemis E A (Jul. 1996). "Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae". Mol. Cell. Biol. (UNITED STATES) 16 (7): 3327–37. ISSN 0270-7306. PMC 231327. PMID 8668148. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231327.
^ Kovacic-Milivojević, B; Roediger F, Almeida E A, Damsky C H, Gardner D G, Ilić D (Aug. 2001). "Focal Adhesion Kinase and p130Cas Mediate Both Sarcomeric Organization and Activation of Genes Associated with Cardiac Myocyte Hypertrophy". Mol. Biol. Cell (United States) 12 (8): 2290–307. ISSN 1059-1524. PMC 58595. PMID 11514617. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=58595.
^ Turner, C E; Brown M C, Perrotta J A, Riedy M C, Nikolopoulos S N, McDonald A R, Bagrodia S, Thomas S, Leventhal P S (May. 1999). "Paxillin LD4 Motif Binds PAK and PIX through a Novel 95-kD Ankyrin Repeat, ARF–GAP Protein: A Role in Cytoskeletal Remodeling". J. Cell Biol. (UNITED STATES) 145 (4): 851–63. doi:10.1083/jcb.145.4.851. ISSN 0021-9525. PMC 2133183. PMID 10330411. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133183.
^ Liu, Shouchun; Kiosses William B, Rose David M, Slepak Marina, Salgia Ravi, Griffin James D, Turner Christopher E, Schwartz Martin A, Ginsberg Mark H (Jun. 2002). "A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration". J. Biol. Chem. (United States) 277 (23): 20887–94. doi:10.1074/jbc.M110928200. ISSN 0021-9258. PMID 11919182.
^ Mazaki, Y; Hashimoto S, Sabe H (Mar. 1997). "Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins". J. Biol. Chem. (UNITED STATES) 272 (11): 7437–44. doi:10.1074/jbc.272.11.7437. ISSN 0021-9258. PMID 9054445.
^ Brown, M C; Perrotta J A, Turner C E (Nov. 1996). "Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding". J. Cell Biol. (UNITED STATES) 135 (4): 1109–23. doi:10.1083/jcb.135.4.1109. ISSN 0021-9525. PMC 2133378. PMID 8922390. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133378.
^ Fujita, H; Kamiguchi K, Cho D, Shibanuma M, Morimoto C, Tachibana K (Oct. 1998). "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase". J. Biol. Chem. (UNITED STATES) 273 (41): 26516–21. doi:10.1074/jbc.273.41.26516. ISSN 0021-9258. PMID 9756887.
^ Zhang, Z; Hernandez-Lagunas L, Horne W C, Baron R (Aug. 1999). "Cytoskeleton-dependent tyrosine phosphorylation of the p130(Cas) family member HEF1 downstream of the G protein-coupled calcitonin receptor. Calcitonin induces the association of HEF1, paxillin, and focal adhesion kinase". J. Biol. Chem. (UNITED STATES) 274 (35): 25093–8. doi:10.1074/jbc.274.35.25093. ISSN 0021-9258. PMID 10455189.
^ ^a ^b ^c Angers-Loustau, A; Côté J F, Charest A, Dowbenko D, Spencer S, Lasky L A, Tremblay M L (Mar. 1999). "Protein Tyrosine Phosphatase-PEST Regulates Focal Adhesion Disassembly, Migration, and Cytokinesis in Fibroblasts". J. Cell Biol. (UNITED STATES) 144 (5): 1019–31. doi:10.1083/jcb.144.5.1019. ISSN 0021-9525. PMC 2148201. PMID 10085298. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2148201.
^ ^a ^b Eliceiri, Brian P; Puente Xose S, Hood John D, Stupack Dwayne G, Schlaepfer David D, Huang Xiaozhu Z, Sheppard Dean, Cheresh David A (Apr. 2002). "Src-mediated coupling of focal adhesion kinase to integrin αvβ5 in vascular endothelial growth factor signaling". J. Cell Biol. (United States) 157 (1): 149–60. doi:10.1083/jcb.200109079. ISSN 0021-9525. PMC 2173263. PMID 11927607. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173263.
^ Ko, Jaewon; Kim Seho, Valtschanoff Juli G, Shin Hyewon, Lee Jae-Ran, Sheng Morgan, Premont Richard T, Weinberg Richard J, Kim Eunjoon (Mar. 2003). "Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting". J. Neurosci. (United States) 23 (5): 1667–77. PMID 12629171.
^ Kim, Seho; Ko Jaewon, Shin Hyewon, Lee Jae-Ran, Lim Chunghun, Han Jin-Hee, Altrock Wilko D, Garner Craig C, Gundelfinger Eckart D, Premont Richard T, Kaang Bong-Kiun, Kim Eunjoon (Feb. 2003). "The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo". J. Biol. Chem. (United States) 278 (8): 6291–300. doi:10.1074/jbc.M212287200. ISSN 0021-9258. PMID 12473661.
^ Zhao, Z S; Manser E, Loo T H, Lim L (Sep. 2000). "Coupling of PAK-Interacting Exchange Factor PIX to GIT1 Promotes Focal Complex Disassembly". Mol. Cell. Biol. (UNITED STATES) 20 (17): 6354–63. doi:10.1128/MCB.20.17.6354-6363.2000. ISSN 0270-7306. PMC 86110. PMID 10938112. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86110.
^ ^a ^b Chung, J; Gao A G, Frazier W A (Jun. 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. (UNITED STATES) 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN 0021-9258. PMID 9169439.
^ Xie, B; Zhao J, Kitagawa M, Durbin J, Madri J A, Guan J L, Fu X Y (Jun. 2001). "Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion". J. Biol. Chem. (United States) 276 (22): 19512–23. doi:10.1074/jbc.M009063200. ISSN 0021-9258. PMID 11278462.
^ Tamura, M; Gu J, Danen E H, Takino T, Miyamoto S, Yamada K M (Jul. 1999). "PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway". J. Biol. Chem. (UNITED STATES) 274 (29): 20693–703. doi:10.1074/jbc.274.29.20693. ISSN 0021-9258. PMID 10400703.
^ Haier, Jörg; Nicolson Garth L (Feb. 2002). "PTEN regulates tumor cell adhesion of colon carcinoma cells under dynamic conditions of fluid flow". Oncogene (England) 21 (9): 1450–60. doi:10.1038/sj.onc.1205213. ISSN 0950-9232. PMID 11857088.
^ Hecker, Timothy P; Grammer J Robert, Gillespie G Yancey, Stewart Jerry, Gladson Candece L (May. 2002). "Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples". Cancer Res. (United States) 62 (9): 2699–707. ISSN 0008-5472. PMID 11980671.
^ Relou, Ingrid A M; Bax Liane A B, van Rijn Herman J M, Akkerman Jan-Willem N (Jan. 2003). "Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein". Biochem. J. (England) 369 (Pt 2): 407–16. doi:10.1042/BJ20020410. ISSN 0264-6021. PMC 1223094. PMID 12387730. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223094.
^ ^a ^b ^c Messina, Samantha; Onofri Franco, Bongiorno-Borbone Lucilla, Giovedì Silvia, Valtorta Flavia, Girault Jean-Antoine, Benfenati Fabio (Jan. 2003). "Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin". J. Neurochem. (England) 84 (2): 253–65. doi:10.1046/j.1471-4159.2003.01519.x. ISSN 0022-3042. PMID 12558988.
^ ^a ^b Lebrun, P; Mothe-Satney I, Delahaye L, Van Obberghen E, Baron V (Nov. 1998). "Insulin receptor substrate-1 as a signaling molecule for focal adhesion kinase pp125(FAK) and pp60(src)". J. Biol. Chem. (UNITED STATES) 273 (48): 32244–53. doi:10.1074/jbc.273.48.32244. ISSN 0021-9258. PMID 9822703.
^ Chen, R; Kim O, Li M, Xiong X, Guan J L, Kung H J, Chen H, Shimizu Y, Qiu Y (May. 2001). "Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain". Nat. Cell Biol. (England) 3 (5): 439–44. doi:10.1038/35074500. ISSN 1465-7392. PMID 11331870.
^ Sieg, D J; Hauck C R, Ilic D, Klingbeil C K, Schaefer E, Damsky C H, Schlaepfer D D (May. 2000). "FAK integrates growth-factor and integrin signals to promote cell migration". Nat. Cell Biol. (ENGLAND) 2 (5): 249–56. doi:10.1038/35010517. ISSN 1465-7392. PMID 10806474.
^ Arold, Stefan T; Hoellerer Maria K, Noble Martin E M (Mar. 2002). "The structural basis of localization and signaling by the focal adhesion targeting domain". Structure (United States) 10 (3): 319–27. doi:10.1016/S0969-2126(02)00717-7. ISSN 0969-2126. PMID 12005431.
^ Han, D C; Guan J L (Aug. 1999). "Association of focal adhesion kinase with Grb7 and its role in cell migration". J. Biol. Chem. (UNITED STATES) 274 (34): 24425–30. doi:10.1074/jbc.274.34.24425. ISSN 0021-9258. PMID 10446223.
^ Ueda, H; Abbi S, Zheng C, Guan J L (Apr. 2000). "Suppression of Pyk2 Kinase and Cellular Activities by Fip200". J. Cell Biol. (UNITED STATES) 149 (2): 423–30. doi:10.1083/jcb.149.2.423. ISSN 0021-9525. PMC 2175150. PMID 10769033. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175150.
^ Sada, K; Minami Y, Yamamura H (Sep. 1997). "Relocation of Syk protein-tyrosine kinase to the actin filament network and subsequent association with Fak". Eur. J. Biochem. (GERMANY) 248 (3): 827–33. doi:10.1111/j.1432-1033.1997.00827.x. ISSN 0014-2956. PMID 9342235.
^ Arold, S T; Ulmer T S, Mulhern T D, Werner J M, Ladbury J E, Campbell I D, Noble M E (May. 2001). "The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases". J. Biol. Chem. (United States) 276 (20): 17199–205. doi:10.1074/jbc.M011185200. ISSN 0021-9258. PMID 11278857.
^ Lim, Ssang-Taek; Chen Xiao Lei, Lim Yangmi, Hanson Dan A, Vo Thanh-Trang, Howerton Kyle, Larocque Nicholas, Fisher Susan J, Schlaepfer David D, Ilic Dusko (Jan. 2008). "Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation". Mol. Cell (United States) 29 (1): 9–22. doi:10.1016/j.molcel.2007.11.031. ISSN 1097-2765. PMC 2234035. PMID 18206965. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2234035.
^ Takino, Takahisa; Yoshioka Katsuji, Miyamori Hisashi, Yamada Kenneth M, Sato Hiroshi (Sep. 2002). "A scaffold protein in the c-Jun N-terminal kinase signaling pathway is associated with focal adhesion kinase and tyrosine-phosphorylated". Oncogene (England) 21 (42): 6488–97. doi:10.1038/sj.onc.1205840. ISSN 0950-9232. PMID 12226752.

External links

MBInfo: FAK
FAK Info with links in the Cell Migration Gateway
MeSH protein, human PTK2 protein, human

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 巣状分節性糸球体硬化症の疫学、分類、および病因 epidemiology classification and pathogenesis of focal segmental glomerulosclerosis
2. 慢性骨髄性白血病の細胞生物学および分子生物学 cellular and molecular biology of chronic myeloid leukemia
3. 炎症の病因における白血球内皮細胞接着 leukocyte endothelial adhesion in the pathogenesis of inflammation
4. Leukocyte-adhesion deficiency
5. 心筋障害のバイオマーカーとしてのトロポニンおよびクレアチンキナーゼ troponins and creatine kinase as biomarkers of cardiac injury

English Journal

Loss of focal adhesions in glia disrupts both glial and photoreceptor axon migration in the Drosophila visual system.

Xie X1, Gilbert M1, Petley-Ragan L1, Auld VJ2.
Development (Cambridge, England).Development.2014 Aug;141(15):3072-83. doi: 10.1242/dev.101972.
Many aspects of glial development are regulated by extracellular signals, including those from the extracellular matrix (ECM). Signals from the ECM are received by cell surface receptors, including the integrin family. Previously, we have shown that Drosophila integrins form adhesion complexes with
PMID 25053436

Matriptase is required for the active form of hepatocyte growth factor induced Met, focal adhesion kinase and protein kinase B activation on neural stem/progenitor cell motility.

Fang JD1, Lee SL2.
Biochimica et biophysica acta.Biochim Biophys Acta.2014 Jul;1843(7):1285-94. doi: 10.1016/j.bbamcr.2014.03.020. Epub 2014 Mar 28.
Hepatocyte growth factor (HGF) is a chemoattractant and inducer for neural stem/progenitor (NS/P) cell migration. Although the type II transmembrane serine protease, matriptase (MTP) is an activator of the latent HGF, MTP is indispensable on NS/P cell motility induced by the active form of HGF. This
PMID 24685580

Analyses of merlin/NF2 connection to FAK inhibitor responsiveness in serous ovarian cancer.

Shah NR1, Tancioni I1, Ward KK1, Lawson C1, Chen XL1, Jean C1, Sulzmaier FJ1, Uryu S1, Miller NL1, Connolly DC2, Schlaepfer DD3.
Gynecologic oncology.Gynecol Oncol.2014 Jul;134(1):104-11. doi: 10.1016/j.ygyno.2014.04.044. Epub 2014 Apr 27.
OBJECTIVE: Focal adhesion kinase (FAK) is overexpressed in serous ovarian cancer. Loss of merlin, a product of the neurofibromatosis 2 tumor suppressor gene, is being evaluated as a biomarker for FAK inhibitor sensitivity in mesothelioma. Connections between merlin and FAK in ovarian cancer remain u
PMID 24786638

Japanese Journal

Endothelial Cell Migration was Impaired by Irradiation-Induced Inhibition of SHP-2 in Radiotherapy: an In vitro Study

ZHENG Xiangpeng,MOHAN Sumathy,OTTO Randal A.,NATARAJAN Mohan
Journal of Radiation Research 52(3), 320-328, 2011
… The expression of αvβ3 integrins, focal adhesion kinase (FAK) and phosphorylated FAK (tyr397) as well as SHP-2 phosphatase were assayed through immunoblotting, immunoprecipitation and optical imaging. …
NAID 130000673655

Hypertension Promotes Phosphorylation of Focal Adhesion Kinase and Proline-Rich Tyrosine Kinase 2 in Rats : Implication for the Pathogenesis of Hypertensive Vascular Disease

SUGIMURA Koichiro,FUKUMOTO Yoshihiro,NAWATA Jun,WANG Huan,ONOUE Noriko,TADA Tomohiro,SHIRATO Kunio,SHIMOKAWA Hiroaki
Tohoku journal of experimental medicine 222(3), 201-210, 2010-11-01
NAID 10027459508

「接着斑キナーゼ1」

PTK2 protein tyrosine kinase 2
	; PDB rendering based on 1k04.
Available structures
PDB	1K04, 1K05, 1MP8, 1OW6, 1OW7, 1OW8, 2ETM, 2IJM, 2RA7, 3B71, 3BZ3
Identifiers
Symbols	PTK2; FADK; FAK; FAK1; FRNK; PPP1R71; p125FAK; pp125FAK
External IDs	OMIM: 600758 MGI: 95481 HomoloGene: 7314 GeneCards: PTK2 Gene
EC number	2.7.10.2
Gene Ontology
Molecular function	• nucleotide binding; • protein kinase activity; • protein tyrosine kinase activity; • non-membrane spanning protein tyrosine kinase activity; • signal transducer activity; • binding; • protein binding; • ATP binding; • JUN kinase binding; • protein kinase binding; • SH2 domain binding;
Cellular component	• nucleus; • cytoplasm; • microtubule organizing center; • cytosol; • cytosol; • cytoskeleton; • plasma membrane; • focal adhesion; • focal adhesion; • cell cortex; • apical plasma membrane; • lamellipodium; • cell junction;
Biological process	• microtubule cytoskeleton organization; • angiogenesis; • blood vessel development; • vasculogenesis; • neuron migration; • placenta development; • positive regulation of protein phosphorylation; • heart morphogenesis; • protein phosphorylation; • apoptotic process; • cellular component disassembly involved in apoptosis; • signal complex assembly; • integrin-mediated signaling pathway; • integrin-mediated signaling pathway; • axon guidance; • blood coagulation; • positive regulation of cell proliferation; • regulation of cell shape; • embryo development; • regulation of endothelial cell migration; • positive regulation of phosphatidylinositol 3-kinase cascade; • peptidyl-tyrosine phosphorylation; • central nervous system neuron axonogenesis; • establishment of cell polarity; • platelet activation; • extracellular matrix organization; • positive regulation of cell migration; • regulation of Rho GTPase activity; • regulation of cell adhesion mediated by integrin; • netrin-activated signaling pathway; • establishment of nucleus localization; • regulation of cell proliferation; • negative regulation of apoptotic process; • positive regulation of phosphatidylinositol 3-kinase activity; • regulation of osteoblast differentiation; • positive regulation of protein kinase activity; • negative regulation of organ growth; • protein autophosphorylation; • ephrin receptor signaling pathway; • cell motility; • negative regulation of axonogenesis; • regulation of cytoskeleton organization; • regulation of focal adhesion assembly; • positive regulation of protein kinase B signaling cascade; • negative regulation of synapse assembly; • growth hormone receptor signaling pathway; • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: focal adhesion kinase 1

「focal」

　　[★]

adj.

焦点の、焦点を通る
(病変が)限局性の、局所の、病巣の、巣状の

関: circumscribed、definite、focal point、focally、foci、focus、local、localized、locally、nidal、nidus、topical、topically

「adhesion」

　　[★]

n

接着、付着、粘着、粘着力、凝着、密着、溶着、癒着、支持、索状帯。固守、執着

「focal adhesion」

　　[★]

接着点、接着斑

関: adhesion plaque、desmosomal、desmosome、focal contact

「kinase」

　　[★] キナーゼカイネースリン酸化酵素 phosphoenzyme phosphotransferase 　

[0] PMID 12005431 (PubMed)
Citation will be completed automatically in a few minutes. Jump the queue or expand by hand

[pmid8422239-1] André E, Becker-André M (January 1993). "Expression of an N-terminally truncated form of human focal adhesion kinase in brain". Biochemical and biophysical research communications 190 (1): 140–7. doi:10.1006/bbrc.1993.1022. PMID 8422239.

[isbn0-12-432565-3-2] Blackshaw, S. E.; Dow, J. Kamal; Lackie, J. M. (1999). The dictionary of cell and molecular biology (3rd ed.). San Diego: Academic Press. ISBN 0-12-432565-3.

[3] Physorg:When cancer cells can't let go

[4] "Entrez Gene: PTK2 PTK2 protein tyrosine kinase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5747.

[pmid1379699-5] Guan JL, Shalloway D (August 1992). "Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation". Nature 358 (6388): 690–2. doi:10.1038/358690a0. PMID 1379699.

[pmid8682874-6] Chrzanowska-Wodnicka M, Burridge K (June 1996). "Rho-stimulated contractility drives the formation of stress fibers and focal adhesions". The Journal of cell biology 133 (6): 1403–15. doi:10.1083/jcb.133.6.1403. PMC 2120895. PMID 8682874. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120895.

[pmid9182576-7] Abedi H, Zachary I (June 1997). "Vascular endothelial growth factor stimulates tyrosine phosphorylation and recruitment to new focal adhesions of focal adhesion kinase and paxillin in endothelial cells". The Journal of biological chemistry 272 (24): 15442–51. doi:10.1074/jbc.272.24.15442. PMID 9182576.

[pmid1458538-8] Zachary I, Rozengurt E (December 1992). "Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes". Cell 71 (6): 891–4. doi:10.1016/0092-8674(92)90385-P. PMID 1458538.

[pmid3058164-9] Burridge K, Fath K, Kelly T, Nuckolls G, Turner C (1988). "Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton". Annual review of cell biology 4: 487–525. doi:10.1146/annurev.cb.04.110188.002415. PMID 3058164.

[pmid1385444-10] Burridge K, Turner CE, Romer LH (November 1992). "Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly". The Journal of cell biology 119 (4): 893–903. doi:10.1083/jcb.119.4.893. PMC 2289706. PMID 1385444. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289706.

[pmid8227154-11] Hildebrand JD, Schaller MD, Parsons JT (November 1993). "Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions". The Journal of cell biology 123 (4): 993–1005. doi:10.1083/jcb.123.4.993. PMC 2200138. PMID 8227154. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2200138.

[pmid7579684-12] Hildebrand JD, Schaller MD, Parsons JT (1 June 1995). "Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase". Molecular biology of the cell 6 (6): 637–47. PMC 301225. PMID 7579684. http://www.molbiolcell.org/cgi/content/abstract/6/6/637.

[pmid7657702-13] Schaller MD, Otey CA, Hildebrand JD, Parsons JT (September 1995). "Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains". The Journal of cell biology 130 (5): 1181–7. doi:10.1083/jcb.130.5.1181. PMC 2120552. PMID 7657702. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120552.

[pmid9065456-14] Tahiliani PD, Singh L, Auer KL, LaFlamme SE (March 1997). "The role of conserved amino acid motifs within the integrin beta3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation". The Journal of biological chemistry 272 (12): 7892–8. doi:10.1074/jbc.272.12.7892. PMID 9065456.

[pmid9990861-15] Girault JA, Labesse G, Mornon JP, Callebaut I (December 1998). "Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction". Molecular medicine (Cambridge, Mass.) 4 (12): 751–69. PMC 2230389. PMID 9990861. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2230389.

[pmid7529876-16] Calalb MB, Polte TR, Hanks SK (1 February 1995). "Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases". Molecular and cellular biology 15 (2): 954–63. PMC 231984. PMID 7529876. http://mcb.asm.org/cgi/content/abstract/15/2/954.

[pmid17043358-17] Gan, Boyi; Yoo Youngdong, Guan Jun-Lin (Dec. 2006). "Association of focal adhesion kinase with tuberous sclerosis complex 2 in the regulation of s6 kinase activation and cell growth". J. Biol. Chem. (United States) 281 (49): 37321–9. doi:10.1074/jbc.M605241200. ISSN 0021-9258. PMID 17043358.

[pmid8879209-18] Minegishi, M; Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (Oct. 1996). "Structure and function of Cas-L, a 105-kD Crk-associated substrate- related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes". J. Exp. Med. (UNITED STATES) 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. ISSN 0022-1007. PMC 2192828. PMID 8879209. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2192828.

[pmid11950595-19] Goicoechea, Silvia M; Tu Yizeng, Hua Yun, Chen Ka, Shen Tang-Long, Guan Jun-Lin, Wu Chuanyue (Jul. 2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". Int. J. Biochem. Cell Biol. (England) 34 (7): 791–805. doi:10.1016/S1357-2725(02)00002-X. ISSN 1357-2725. PMID 11950595.

[pmid9553131-20] Zhu, T; Goh E L, Lobie P E (Apr. 1998). "Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription". J. Biol. Chem. (UNITED STATES) 273 (17): 10682–9. doi:10.1074/jbc.273.17.10682. ISSN 0021-9258. PMID 9553131.

[pmid10925297-21] Ryu, H; Lee J H, Kim K S, Jeong S M, Kim P H, Chung H T (Aug. 2000). "Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin". J. Immunol. (UNITED STATES) 165 (4): 2116–23. ISSN 0022-1767. PMID 10925297.

[pmid7622520-22] Chen, H C; Appeddu P A, Parsons J T, Hildebrand J D, Schaller M D, Guan J L (Jul. 1995). "Interaction of focal adhesion kinase with cytoskeletal protein talin". J. Biol. Chem. (UNITED STATES) 270 (28): 16995–9. doi:10.1074/jbc.270.28.16995. ISSN 0021-9258. PMID 7622520.

[pmid9442086-23] Zheng, C; Xing Z, Bian Z C, Guo C, Akbay A, Warner L, Guan J L (Jan. 1998). "Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion". J. Biol. Chem. (UNITED STATES) 273 (4): 2384–9. doi:10.1074/jbc.273.4.2384. ISSN 0021-9258. PMID 9442086.

[pmid9422762-24] Matsuya, M; Sasaki H, Aoto H, Mitaka T, Nagura K, Ohba T, Ishino M, Takahashi S, Suzuki R, Sasaki T (Jan. 1998). "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". J. Biol. Chem. (UNITED STATES) 273 (2): 1003–14. doi:10.1074/jbc.273.2.1003. ISSN 0021-9258. PMID 9422762.

[pmid11463817-25] Nishiya, N; Tachibana K, Shibanuma M, Mashimo J I, Nose K (Aug. 2001). "Hic-5-Reduced Cell Spreading on Fibronectin: Competitive Effects between Paxillin and Hic-5 through Interaction with Focal Adhesion Kinase". Mol. Cell. Biol. (United States) 21 (16): 5332–45. doi:10.1128/MCB.21.16.5332-5345.2001. ISSN 0270-7306. PMC 87257. PMID 11463817. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=87257.

[pmid9858471-26] Thomas, S M; Hagel M, Turner C E (Jan. 1999). "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". J. Cell. Sci. (ENGLAND) 112 (2): 181–90. ISSN 0021-9533. PMID 9858471.

[pmid8810278-27] Salgia, R; Pisick E, Sattler M, Li J L, Uemura N, Wong W K, Burky S A, Hirai H, Chen L B, Griffin J D (Oct. 1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". J. Biol. Chem. (UNITED STATES) 271 (41): 25198–203. doi:10.1074/jbc.271.41.25198. ISSN 0021-9258. PMID 8810278.

[pmid12615911-28] Hsia, Datsun A; Mitra Satyajit K, Hauck Christof R, Streblow Daniel N, Nelson Jay A, Ilic Dusko, Huang Shuang, Li Erguang, Nemerow Glen R, Leng Jay, Spencer Kathryn S R, Cheresh David A, Schlaepfer David D (Mar. 2003). "Differential regulation of cell motility and invasion by FAK". J. Cell Biol. (United States) 160 (5): 753–67. doi:10.1083/jcb.200212114. ISSN 0021-9525. PMC 2173366. PMID 12615911. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173366.

[pmid8649427-29] Hildebrand, J D; Taylor J M, Parsons J T (Jun. 1996). "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase". Mol. Cell. Biol. (UNITED STATES) 16 (6): 3169–78. ISSN 0270-7306. PMC 231310. PMID 8649427. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231310.

[pmid11577104-30] Chellaiah, M A; Biswas R S, Yuen D, Alvarez U M, Hruska K A (Dec. 2001). "Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin". J. Biol. Chem. (United States) 276 (50): 47434–44. doi:10.1074/jbc.M107494200. ISSN 0021-9258. PMID 11577104.

[pmid12135674-31] Okabe, Seiichi; Fukuda Seiji, Broxmeyer Hal E (Jul. 2002). "Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in a T-lymphocyte line". Exp. Hematol. (Netherlands) 30 (7): 761–6. doi:10.1016/S0301-472X(02)00823-8. ISSN 0301-472X. PMID 12135674.

[pmid10753828-32] Wang, J F; Park I W, Groopman J E (Apr. 2000). "Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood (UNITED STATES) 95 (8): 2505–13. ISSN 0006-4971. PMID 10753828.

[pmid15494733-33] Ren, Xiu-Rong; Ming Guo-Li, Xie Yi, Hong Yan, Sun Dong-Mei, Zhao Zhong-Qiu, Feng Zhu, Wang Qiang, Shim Sangwoo, Chen Zhou-Feng, Song Hong-Jun, Mei Lin, Xiong Wen-Cheng (Nov. 2004). "Focal adhesion kinase in netrin-1 signaling". Nat. Neurosci. (United States) 7 (11): 1204–12. doi:10.1038/nn1330. ISSN 1097-6256. PMID 15494733.

[pmid7537275-34] Guinebault, C; Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H (May. 1995). "Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase". J. Cell Biol. (UNITED STATES) 129 (3): 831–42. doi:10.1083/jcb.129.3.831. ISSN 0021-9525. PMC 2120444. PMID 7537275. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120444.

[pmid8668148-35] Law, S F; Estojak J, Wang B, Mysliwiec T, Kruh G, Golemis E A (Jul. 1996). "Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae". Mol. Cell. Biol. (UNITED STATES) 16 (7): 3327–37. ISSN 0270-7306. PMC 231327. PMID 8668148. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231327.

[pmid11514617-36] Kovacic-Milivojević, B; Roediger F, Almeida E A, Damsky C H, Gardner D G, Ilić D (Aug. 2001). "Focal Adhesion Kinase and p130Cas Mediate Both Sarcomeric Organization and Activation of Genes Associated with Cardiac Myocyte Hypertrophy". Mol. Biol. Cell (United States) 12 (8): 2290–307. ISSN 1059-1524. PMC 58595. PMID 11514617. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=58595.

[pmid10330411-37] Turner, C E; Brown M C, Perrotta J A, Riedy M C, Nikolopoulos S N, McDonald A R, Bagrodia S, Thomas S, Leventhal P S (May. 1999). "Paxillin LD4 Motif Binds PAK and PIX through a Novel 95-kD Ankyrin Repeat, ARF–GAP Protein: A Role in Cytoskeletal Remodeling". J. Cell Biol. (UNITED STATES) 145 (4): 851–63. doi:10.1083/jcb.145.4.851. ISSN 0021-9525. PMC 2133183. PMID 10330411. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133183.

[pmid11919182-38] Liu, Shouchun; Kiosses William B, Rose David M, Slepak Marina, Salgia Ravi, Griffin James D, Turner Christopher E, Schwartz Martin A, Ginsberg Mark H (Jun. 2002). "A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration". J. Biol. Chem. (United States) 277 (23): 20887–94. doi:10.1074/jbc.M110928200. ISSN 0021-9258. PMID 11919182.

[pmid9054445-39] Mazaki, Y; Hashimoto S, Sabe H (Mar. 1997). "Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins". J. Biol. Chem. (UNITED STATES) 272 (11): 7437–44. doi:10.1074/jbc.272.11.7437. ISSN 0021-9258. PMID 9054445.

[pmid8922390-40] Brown, M C; Perrotta J A, Turner C E (Nov. 1996). "Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding". J. Cell Biol. (UNITED STATES) 135 (4): 1109–23. doi:10.1083/jcb.135.4.1109. ISSN 0021-9525. PMC 2133378. PMID 8922390. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133378.

[pmid9756887-41] Fujita, H; Kamiguchi K, Cho D, Shibanuma M, Morimoto C, Tachibana K (Oct. 1998). "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase". J. Biol. Chem. (UNITED STATES) 273 (41): 26516–21. doi:10.1074/jbc.273.41.26516. ISSN 0021-9258. PMID 9756887.

[pmid10455189-42] Zhang, Z; Hernandez-Lagunas L, Horne W C, Baron R (Aug. 1999). "Cytoskeleton-dependent tyrosine phosphorylation of the p130(Cas) family member HEF1 downstream of the G protein-coupled calcitonin receptor. Calcitonin induces the association of HEF1, paxillin, and focal adhesion kinase". J. Biol. Chem. (UNITED STATES) 274 (35): 25093–8. doi:10.1074/jbc.274.35.25093. ISSN 0021-9258. PMID 10455189.

[pmid10085298-43] Angers-Loustau, A; Côté J F, Charest A, Dowbenko D, Spencer S, Lasky L A, Tremblay M L (Mar. 1999). "Protein Tyrosine Phosphatase-PEST Regulates Focal Adhesion Disassembly, Migration, and Cytokinesis in Fibroblasts". J. Cell Biol. (UNITED STATES) 144 (5): 1019–31. doi:10.1083/jcb.144.5.1019. ISSN 0021-9525. PMC 2148201. PMID 10085298. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2148201.

[pmid11927607-44] Eliceiri, Brian P; Puente Xose S, Hood John D, Stupack Dwayne G, Schlaepfer David D, Huang Xiaozhu Z, Sheppard Dean, Cheresh David A (Apr. 2002). "Src-mediated coupling of focal adhesion kinase to integrin αvβ5 in vascular endothelial growth factor signaling". J. Cell Biol. (United States) 157 (1): 149–60. doi:10.1083/jcb.200109079. ISSN 0021-9525. PMC 2173263. PMID 11927607. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173263.

[pmid12629171-45] Ko, Jaewon; Kim Seho, Valtschanoff Juli G, Shin Hyewon, Lee Jae-Ran, Sheng Morgan, Premont Richard T, Weinberg Richard J, Kim Eunjoon (Mar. 2003). "Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting". J. Neurosci. (United States) 23 (5): 1667–77. PMID 12629171.

[pmid12473661-46] Kim, Seho; Ko Jaewon, Shin Hyewon, Lee Jae-Ran, Lim Chunghun, Han Jin-Hee, Altrock Wilko D, Garner Craig C, Gundelfinger Eckart D, Premont Richard T, Kaang Bong-Kiun, Kim Eunjoon (Feb. 2003). "The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo". J. Biol. Chem. (United States) 278 (8): 6291–300. doi:10.1074/jbc.M212287200. ISSN 0021-9258. PMID 12473661.

[pmid10938112-47] Zhao, Z S; Manser E, Loo T H, Lim L (Sep. 2000). "Coupling of PAK-Interacting Exchange Factor PIX to GIT1 Promotes Focal Complex Disassembly". Mol. Cell. Biol. (UNITED STATES) 20 (17): 6354–63. doi:10.1128/MCB.20.17.6354-6363.2000. ISSN 0270-7306. PMC 86110. PMID 10938112. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86110.

[pmid9169439-48] Chung, J; Gao A G, Frazier W A (Jun. 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. (UNITED STATES) 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN 0021-9258. PMID 9169439.

[pmid11278462-49] Xie, B; Zhao J, Kitagawa M, Durbin J, Madri J A, Guan J L, Fu X Y (Jun. 2001). "Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion". J. Biol. Chem. (United States) 276 (22): 19512–23. doi:10.1074/jbc.M009063200. ISSN 0021-9258. PMID 11278462.

[pmid10400703-50] Tamura, M; Gu J, Danen E H, Takino T, Miyamoto S, Yamada K M (Jul. 1999). "PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway". J. Biol. Chem. (UNITED STATES) 274 (29): 20693–703. doi:10.1074/jbc.274.29.20693. ISSN 0021-9258. PMID 10400703.

[pmid11857088-51] Haier, Jörg; Nicolson Garth L (Feb. 2002). "PTEN regulates tumor cell adhesion of colon carcinoma cells under dynamic conditions of fluid flow". Oncogene (England) 21 (9): 1450–60. doi:10.1038/sj.onc.1205213. ISSN 0950-9232. PMID 11857088.

[pmid11980671-52] Hecker, Timothy P; Grammer J Robert, Gillespie G Yancey, Stewart Jerry, Gladson Candece L (May. 2002). "Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples". Cancer Res. (United States) 62 (9): 2699–707. ISSN 0008-5472. PMID 11980671.

[pmid12387730-53] Relou, Ingrid A M; Bax Liane A B, van Rijn Herman J M, Akkerman Jan-Willem N (Jan. 2003). "Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein". Biochem. J. (England) 369 (Pt 2): 407–16. doi:10.1042/BJ20020410. ISSN 0264-6021. PMC 1223094. PMID 12387730. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223094.

[pmid12558988-54] Messina, Samantha; Onofri Franco, Bongiorno-Borbone Lucilla, Giovedì Silvia, Valtorta Flavia, Girault Jean-Antoine, Benfenati Fabio (Jan. 2003). "Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin". J. Neurochem. (England) 84 (2): 253–65. doi:10.1046/j.1471-4159.2003.01519.x. ISSN 0022-3042. PMID 12558988.

[pmid9822703-55] Lebrun, P; Mothe-Satney I, Delahaye L, Van Obberghen E, Baron V (Nov. 1998). "Insulin receptor substrate-1 as a signaling molecule for focal adhesion kinase pp125(FAK) and pp60(src)". J. Biol. Chem. (UNITED STATES) 273 (48): 32244–53. doi:10.1074/jbc.273.48.32244. ISSN 0021-9258. PMID 9822703.

[pmid11331870-56] Chen, R; Kim O, Li M, Xiong X, Guan J L, Kung H J, Chen H, Shimizu Y, Qiu Y (May. 2001). "Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain". Nat. Cell Biol. (England) 3 (5): 439–44. doi:10.1038/35074500. ISSN 1465-7392. PMID 11331870.

[pmid10806474-57] Sieg, D J; Hauck C R, Ilic D, Klingbeil C K, Schaefer E, Damsky C H, Schlaepfer D D (May. 2000). "FAK integrates growth-factor and integrin signals to promote cell migration". Nat. Cell Biol. (ENGLAND) 2 (5): 249–56. doi:10.1038/35010517. ISSN 1465-7392. PMID 10806474.

[pmid12005431-58] Arold, Stefan T; Hoellerer Maria K, Noble Martin E M (Mar. 2002). "The structural basis of localization and signaling by the focal adhesion targeting domain". Structure (United States) 10 (3): 319–27. doi:10.1016/S0969-2126(02)00717-7. ISSN 0969-2126. PMID 12005431.

[pmid10446223-59] Han, D C; Guan J L (Aug. 1999). "Association of focal adhesion kinase with Grb7 and its role in cell migration". J. Biol. Chem. (UNITED STATES) 274 (34): 24425–30. doi:10.1074/jbc.274.34.24425. ISSN 0021-9258. PMID 10446223.

[pmid10769033-60] Ueda, H; Abbi S, Zheng C, Guan J L (Apr. 2000). "Suppression of Pyk2 Kinase and Cellular Activities by Fip200". J. Cell Biol. (UNITED STATES) 149 (2): 423–30. doi:10.1083/jcb.149.2.423. ISSN 0021-9525. PMC 2175150. PMID 10769033. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175150.

[pmid9342235-61] Sada, K; Minami Y, Yamamura H (Sep. 1997). "Relocation of Syk protein-tyrosine kinase to the actin filament network and subsequent association with Fak". Eur. J. Biochem. (GERMANY) 248 (3): 827–33. doi:10.1111/j.1432-1033.1997.00827.x. ISSN 0014-2956. PMID 9342235.

[pmid11278857-62] Arold, S T; Ulmer T S, Mulhern T D, Werner J M, Ladbury J E, Campbell I D, Noble M E (May. 2001). "The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases". J. Biol. Chem. (United States) 276 (20): 17199–205. doi:10.1074/jbc.M011185200. ISSN 0021-9258. PMID 11278857.

[pmid18206965-63] Lim, Ssang-Taek; Chen Xiao Lei, Lim Yangmi, Hanson Dan A, Vo Thanh-Trang, Howerton Kyle, Larocque Nicholas, Fisher Susan J, Schlaepfer David D, Ilic Dusko (Jan. 2008). "Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation". Mol. Cell (United States) 29 (1): 9–22. doi:10.1016/j.molcel.2007.11.031. ISSN 1097-2765. PMC 2234035. PMID 18206965. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2234035.

[pmid12226752-64] Takino, Takahisa; Yoshioka Katsuji, Miyamori Hisashi, Yamada Kenneth M, Sato Hiroshi (Sep. 2002). "A scaffold protein in the c-Jun N-terminal kinase signaling pathway is associated with focal adhesion kinase and tyrosine-phosphorylated". Oncogene (England) 21 (42): 6488–97. doi:10.1038/sj.onc.1205840. ISSN 0950-9232. PMID 12226752.

リンク元	「接着斑キナーゼ1」
関連記事	「focal」「adhesion」「focal adhesion」「kinase」

匿名

検索

案内

案内

focal adhesion kinase 1