パキシリン
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/03/04 23:13:36」(JST)
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Not to be confused with the neurotoxin paxilline.
Paxillin |
Rendering based on PDB 1KKY. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1KKY, 1KL0, 1OW6, 1OW7, 1OW8, 2K2R, 2O9V, 2VZD, 2VZG, 2VZI, 3GM1, 3PY7, 3RQE, 3RQF, 3RQG, 3U3C, 3U3F, 4EDN
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Identifiers |
Symbols |
PXN ; FLJ16691 |
External IDs |
OMIM: 602505 MGI: 108295 HomoloGene: 37697 ChEMBL: 5715 GeneCards: PXN Gene |
Gene ontology |
Molecular function |
• integrin binding
• protein binding
• beta-catenin binding
• zinc ion binding
• vinculin binding
• protein kinase binding
• BH4 domain binding
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Cellular component |
• nucleus
• nucleolus
• cytoplasm
• microtubule associated complex
• plasma membrane
• focal adhesion
• cell cortex
• lamellipodium
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Biological process |
• activation of MAPK activity
• cellular component movement
• muscle contraction
• cytoskeleton organization
• cell adhesion
• signal transduction
• signal complex assembly
• epidermal growth factor receptor signaling pathway
• integrin-mediated signaling pathway
• peptidyl-tyrosine phosphorylation
• lamellipodium assembly
• cell junction assembly
• cellular response to reactive oxygen species
• focal adhesion assembly
• branching morphogenesis of an epithelial tube
• growth hormone receptor signaling pathway
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Sources: Amigo / QuickGO |
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Orthologs |
Species |
Human |
Mouse |
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Entrez |
5829 |
19303 |
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Ensembl |
ENSG00000089159 |
ENSMUSG00000029528 |
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UniProt |
P49023 |
Q8VI36 |
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RefSeq (mRNA) |
NM_001080855 |
NM_011223 |
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RefSeq (protein) |
NP_001074324 |
NP_035353 |
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Location (UCSC) |
Chr 12:
120.65 – 120.7 Mb |
Chr 5:
115.51 – 115.56 Mb |
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PubMed search |
[1] |
[2] |
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Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge.[1] The C-terminal region of paxillin contains four LIM domains that target paxillin to focal adhesions. It is presumed through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal region of paxillin is rich in protein–protein interaction sites. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and focal adhesion kinase (FAK), structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT. Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk.[2]
References
- ^ Turner, C. E., Glenney, J. R., Jr. & Burridge, K. Paxillin: a new vinculin-binding protein present in focal adhesions. J Cell Biol 111, 1059–1068 (1990).
- ^ From the Cell Migration Knowledgebase
Further reading
- Turner CE (1998). "Paxillin.". Int. J. Biochem. Cell Biol. 30 (9): 955–59. doi:10.1016/S1357-2725(98)00062-4. PMID 9785458.
- Panetti TS (2002). "Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.". Front. Biosci. 7: d143–50. doi:10.2741/panetti. PMID 11779709.
- Rose DM, Han J, Ginsberg MH (2003). "Alpha4 integrins and the immune response.". Immunol. Rev. 186: 118–24. doi:10.1034/j.1600-065X.2002.18611.x. PMID 12234367.
- Salgia R; Uemura N; Okuda K et al. (1996). "CRKL links p210BCR/ABL with paxillin in chronic myelogenous leukemia cells". J. Biol. Chem. 270 (49): 29145–50. doi:10.1074/jbc.270.49.29145. PMID 7493940.
- Turner CE, Miller JT (1994). "Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region". J. Cell. Sci. 107 (6): 1583–91. PMID 7525621.
- Bergman M, Joukov V, Virtanen I, Alitalo K (1995). "Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading". Mol. Cell. Biol. 15 (2): 711–22. PMC 231937. PMID 7529872.
- Salgia R; Li JL; Lo SH et al. (1995). "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL". J. Biol. Chem. 270 (10): 5039–47. doi:10.1074/jbc.270.10.5039. PMID 7534286.
- Schaller MD, Otey CA, Hildebrand JD, Parsons JT (1995). "Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains". J. Cell Biol. 130 (5): 1181–7. doi:10.1083/jcb.130.5.1181. PMC 2120552. PMID 7657702.
- Yoshida M; Westlin WF; Wang N et al. (1996). "Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton". J. Cell Biol. 133 (2): 445–55. doi:10.1083/jcb.133.2.445. PMC 2120789. PMID 8609175.
- Salgia R; Sattler M; Pisick E et al. (1996). "p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl". Exp. Hematol. 24 (2): 310–3. PMID 8641358.
- Salgia R; Pisick E; Sattler M et al. (1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". J. Biol. Chem. 271 (41): 25198–203. doi:10.1074/jbc.271.41.25198. PMID 8810278.
- Brown MC, Perrotta JA, Turner CE (1997). "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. 135 (4): 1109–23. doi:10.1083/jcb.135.4.1109. PMC 2133378. PMID 8922390.
- Retta SF; Barry ST; Critchley DR et al. (1997). "Focal adhesion and stress fiber formation is regulated by tyrosine phosphatase activity". Exp. Cell Res. 229 (2): 307–17. doi:10.1006/excr.1996.0376. PMID 8986614.
- Mazaki Y, Hashimoto S, Sabe H (1997). "Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins". J. Biol. Chem. 272 (11): 7437–44. doi:10.1074/jbc.272.11.7437. PMID 9054445.
- Hiregowdara D; Avraham H; Fu Y et al. (1997). "Tyrosine phosphorylation of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation and its association with paxillin". J. Biol. Chem. 272 (16): 10804–10. doi:10.1074/jbc.272.16.10804. PMID 9099734.
- Ostergaard HL, Lou O, Arendt CW, Berg NN (1998). "Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3- or anti-CD45-stimulated T cells". J. Biol. Chem. 273 (10): 5692–6. doi:10.1074/jbc.273.10.5692. PMID 9488700.
- Fernandez R, Suchard SJ (1998). "Syk activation is required for spreading and H2O2 release in adherent human neutrophils". J. Immunol. 160 (10): 5154–62. PMID 9590268.
- Lewis JM, Schwartz MA (1998). "Integrins regulate the association and phosphorylation of paxillin by c-Abl". J. Biol. Chem. 273 (23): 14225–30. doi:10.1074/jbc.273.23.14225. PMID 9603926.
- Ganju RK; Munshi N; Nair BC et al. (1998). "Human Immunodeficiency Virus Tat Modulates the Flk-1/KDR Receptor, Mitogen-Activated Protein Kinases, and Components of Focal Adhesion in Kaposi's Sarcoma Cells". J. Virol. 72 (7): 6131–7. PMC 110419. PMID 9621077.
- Deakin NO, Turner CE (2008). "Paxillin comes of age". J. Cell. Sci. 121 (Pt 15): 2435–44. doi:10.1242/jcs.018044. PMC 2522309. PMID 18650496.
External links
- MBInfo: Paxillin
- Paxillin Info with links in the Cell Migration Gateway
- Paxillin at the US National Library of Medicine Medical Subject Headings (MeSH)
Cell signaling: carrier proteins: signal transducing adaptor proteins
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JAK-STAT |
- see JAK-STAT signaling pathway
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Growth factor receptor-bound protein |
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Other |
- 14-3-3
- Caveolin
- Cortactin
- Death-inducing signaling complex
- Paxillin
- MYD88
- SMAD
- TRAF
- TRAF1
- TRAF2
- TRAF3
- TRAF4
- TRAF5
- TRAF6)
- BIN1
- SH3BP2
- LDB3
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Index of signal transduction
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Description |
Signal transduction:
- Intercellular
- Neuropeptides
- Growth factors
- Cytokines
- Hormones
- Cell surface receptors
- (Ligand-gated
- Enzyme-linked
- G protein-coupled
- Immunoglobulin superfamily
- Integrins
- Neuropeptide
- Growth factor
- Cytokine
- Intracellular
- adaptor proteins
- GTP-binding
- MAP kinase
- Calcium signaling
- Lipid signaling
- Pathways
- Hedgehog
- Wnt
- TGF beta
- MAPK ERK
- Notch
- JAK-STAT
- Apoptosis
- Hippo
- TLR
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UpToDate Contents
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English Journal
- Bupleurum chinense polysaccharide inhibit adhesion of human melanoma cells via blocking β1 integrin function.
- Tong H1, Jiang G2, Qi D3, Bi J4, Tian D5, Guan X5, Zheng S6, Sun X7.
- Carbohydrate polymers.Carbohydr Polym.2017 Jan 20;156:244-252. doi: 10.1016/j.carbpol.2016.09.034. Epub 2016 Sep 13.
- Adhesive interaction contributes toward tumor metastasis and the transmembrane glycoprotein receptor, integrin has been recognized to mediate the adhesion to extracellular matrix thus upregulating tumor metastasis. In the current study, we evaluated the anti-adhesive mechanisms of a water-soluble po
- PMID 27842819
- Polymer fiber-based models of connective tissue repair and healing.
- Lee NM1, Erisken C1, Iskratsch T2, Sheetz M2, Levine WN3, Lu HH4.
- Biomaterials.Biomaterials.2017 Jan;112:303-312. doi: 10.1016/j.biomaterials.2016.10.013. Epub 2016 Oct 12.
- Physiologically relevant models of wound healing are essential for understanding the biology of connective tissue repair and healing. They can also be used to identify key cellular processes and matrix characteristics critical for the design of soft tissue grafts. Modeling the various stages of repa
- PMID 27770633
- Uterine focal adhesions are retained at implantation after rat ovarian hyperstimulation.
- Lindsay LA1, Dowland SN2, Murphy CR2.
- Reproduction (Cambridge, England).Reproduction.2016 Dec;152(6):753-763. Epub 2016 Sep 20.
- Controlled ovarian hyperstimulation is an essential component of IVF techniques to ensure proliferation and development of multiple ovarian follicles, but the effects of these hormones on the endometrium are largely unknown. During normal pregnancy in rats, there are significant changes in the basal
- PMID 27651522
Japanese Journal
- MPC polymer regulates fibrous tissue formation by modulating cell adhesion to the biomaterial surface
- ZHANG Ye,KANETAKA Hiroyasu,SANO Yuya,KANO Mitsuhiro,KUDO Tada-aki,SHIMIZU Yoshinaka
- Dental materials journal 29(5), 518-528, 2010-09-01
- … Furthermore, weaker expressions of paxillin, talin, and ROCK1, but stronger expression of cofilin, were observed in the experimental group. …
- NAID 10026669640
- MT1-MMP promotes cell growth and ERK activation through c-Src and paxillin in three-dimensional collagen matrix
- Takino Takahisa,Tsuge Hisashi,Ozawa Terumasa,Sato Hiroshi
- Biochemical and Biophysical Research Communications 396(4), 1042-1047, 2010-06
- … These MT1-MMP-mediated signal transductions were paxillin dependent, as knockdown of paxillin reduced cell growth and ERK activation, and co-expression of MT1-MMP with paxillin induced ERK activation. … The results suggest that MT1-MMP contributes to proliferation of cancer cells in the extracellular matrix by activating ERK through c-Src and paxillin. …
- NAID 120002224339
- LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin
- TANAKA Toshiyuki,MORIWAKI Kazumasa,MURATA Shinsuke,MIYASAKA Masayuki
- Cancer science 101(2), 363-368, 2010-02-10
- NAID 10026587701
Related Links
- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】Phospho-Paxillin (Tyr118) Antibodyページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】Paxillin Antibodyページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
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