関: abl oncogene、c-abl gene、c-abl proto-oncogene、v-abl gene、v-abl oncogene

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(genetics) a segment of DNA that is involved in producing a polypeptide chain; it can include regions preceding and following the coding DNA as well as introns between the exons; it is considered a unit of heredity; "genes were formerly called factors" (同)cistron, factor
informal term for information; "give me the gen on your new line of computers"

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/19 12:40:57」(JST)

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Abelson murine leukemia viral oncogene homolog 1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL) located on chromosome 9.^[1] c-Abl is sometimes used to refer to the version of the gene found within the mammalian genome, while v-Abl refers to the viral gene.

Function

The ABL1 proto-oncogene encodes a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response. Activity of ABL1 protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns ABL1 into an oncogene. The t(9;22) translocation results in the head-to-tail fusion of the BCR and ABL1 genes, leading to a fusion gene present in many cases of chronic myelogenous leukemia. The DNA-binding activity of the ubiquitously expressed ABL1 tyrosine kinase is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function for ABL1. The ABL1 gene is expressed as either a 6- or a 7-kb mRNA transcript, with alternatively spliced first exons spliced to the common exons 2-11.^[2]

Clinical significance

ABL1 kinase domain (blue) in complex with the second-generation Bcr-Abl tyrosine-kinase inhibitor nilotinib (red)

Mutations in the ABL1 gene are associated with chronic myelogenous leukemia (CML). In CML, the gene is activated by being translocated within the BCR (breakpoint cluster region) gene on chromosome 22. This new fusion gene, BCR-ABL, encodes an unregulated, cytoplasm-targeted tyrosine kinase that allows the cells to proliferate without being regulated by cytokines. This, in turn, allows the cell to become cancerous.

This gene is a partner in a fusion gene with the BCR gene in the Philadelphia chromosome, a characteristic abnormality in chronic myelogenous leukemia (CML) and rarely in some other leukemia forms. The BCR-ABL transcript encodes a tyrosine kinase, which activates mediators of the cell cycle regulation system, leading to a clonal myeloproliferative disorder. The BCR-ABL protein can be inhibited by various small molecules. One such inhibitor is imatinib mesylate, which occupies the tyrosine kinase domain and inhibits BCR-ABL's influence on the cell cycle. Second generation BCR-ABL tyrosine-kinase inhibitors are also under development to inhibit BCR-ABL mutants resistant to imatinib.

Interactions

Abl gene has been shown to interact with:

ABI1,^[3]^[4]^[5]
ABI2,^[6]^[7]
ABL2,^[6]
ATM,^[8]^[9]^[10]
BCAR1,^[11]^[12]
BCR,^[13]^[14]^[15]
BRCA1,^[16]
CAT,^[17]
CBL,^[18]^[19]
CRKL,^[20]^[21]^[22]
DOK1,^[23]^[24]
EPHB2,^[25]
GPX1,^[26]
GRB10,^[27]^[28]
MTOR,^[29]
GRB2,^[20]^[30]
MDM2,^[31]
NCK1,^[18]^[20]
NEDD9,^[32]^[33]
NTRK1,^[34]^[35]
P73,^[36]^[37]
PAG1,^[38]
PAK2,^[39]
PSTPIP1,^[40]
RAD9A,^[41]
RAD51,^[8]
RB1,^[42]^[43]
RFX1,^[44]
RYBP,^[45]
SHC1,^[13]^[46]
SORBS2,^[19]^[47]
SPTA1,^[48]
SPTAN1,^[48]
TERF1,^[10]
VAV1,^[49] and
YTHDC1.^[50]

Regulation

There is some evidence that the expression of Abl is regulated by the microRNA miR-203.^[51]

References

^ Szczylik C, Skorski T, Nicolaides NC, Manzella L, Malaguarnera L, Venturelli D et al. (August 1991). "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science 253 (5019): 562–5. doi:10.1126/science.1857987. PMID 1857987.
^ "Entrez Gene: ABL1 v-abl Abelson murine leukemia viral oncogene homolog 1".
^ Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H et al. (June 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. doi:10.1074/jbc.M301447200. PMID 12672821.
^ Biesova Z, Piccoli C, Wong WT (January 1997). "Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth". Oncogene 14 (2): 233–41. doi:10.1038/sj.onc.1200822. PMID 9010225.
^ Yamamoto A, Suzuki T, Sakaki Y (June 2001). "Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease". Gene 271 (2): 159–69. doi:10.1016/S0378-1119(01)00521-2. PMID 11418237.
^ ^a ^b Cao C, Leng Y, Li C, Kufe D (April 2003). "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response". J. Biol. Chem. 278 (15): 12961–7. doi:10.1074/jbc.M300058200. PMID 12569093.
^ Dai Z, Pendergast AM (November 1995). "Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity". Genes Dev. 9 (21): 2569–82. doi:10.1101/gad.9.21.2569. PMID 7590236.
^ ^a ^b Chen G, Yuan SS, Liu W, Xu Y, Trujillo K, Song B et al. (April 1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". J. Biol. Chem. 274 (18): 12748–52. doi:10.1074/jbc.274.18.12748. PMID 10212258.
^ Shafman T, Khanna KK, Kedar P, Spring K, Kozlov S, Yen T et al. (May 1997). "Interaction between ATM protein and c-Abl in response to DNA damage". Nature 387 (6632): 520–3. doi:10.1038/387520a0. PMID 9168117.
^ ^a ^b Kishi S, Zhou XZ, Ziv Y, Khoo C, Hill DE, Shiloh Y et al. (August 2001). "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks". J. Biol. Chem. 276 (31): 29282–91. doi:10.1074/jbc.M011534200. PMID 11375976.
^ Salgia R, Pisick E, Sattler M, Li JL, Uemura N, Wong WK et al. (October 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.
^ Mayer BJ, Hirai H, Sakai R (March 1995). "Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases". Curr. Biol. 5 (3): 296–305. doi:10.1016/S0960-9822(95)00060-1. PMID 7780740.
^ ^a ^b Puil L, Liu J, Gish G, Mbamalu G, Bowtell D, Pelicci PG et al. (February 1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. 13 (4): 764–73. PMC 394874. PMID 8112292.
^ Ling X, Ma G, Sun T, Liu J, Arlinghaus RB (January 2003). "Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr". Cancer Res. 63 (2): 298–303. PMID 12543778.
^ Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON (July 1991). "BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner". Cell 66 (1): 161–71. doi:10.1016/0092-8674(91)90148-R. PMID 1712671.
^ Foray N, Marot D, Randrianarison V, Venezia ND, Picard D, Perricaudet M et al. (June 2002). "Constitutive association of BRCA1 and c-Abl and its ATM-dependent disruption after irradiation". Mol. Cell. Biol. 22 (12): 4020–32. doi:10.1128/MCB.22.12.4020-4032.2002. PMC 133860. PMID 12024016.
^ Cao C, Leng Y, Kufe D (August 2003). "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". J. Biol. Chem. 278 (32): 29667–75. doi:10.1074/jbc.M301292200. PMID 12777400.
^ ^a ^b Miyoshi-Akiyama T, Aleman LM, Smith JM, Adler CE, Mayer BJ (July 2001). "Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor". Oncogene 20 (30): 4058–69. doi:10.1038/sj.onc.1204528. PMID 11494134.
^ ^a ^b Soubeyran P, Barac A, Szymkiewicz I, Dikic I (February 2003). "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl". Biochem. J. 370 (Pt 1): 29–34. doi:10.1042/BJ20021539. PMC 1223168. PMID 12475393.
^ ^a ^b ^c Ren R, Ye ZS, Baltimore D (April 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes Dev. 8 (7): 783–95. doi:10.1101/gad.8.7.783. PMID 7926767.
^ Heaney C, Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S et al. (January 1997). "Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation". Blood 89 (1): 297–306. PMID 8978305.
^ Kyono WT, de Jong R, Park RK, Liu Y, Heisterkamp N, Groffen J et al. (November 1998). "Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI)". J. Immunol. 161 (10): 5555–63. PMID 9820532.
^ van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Löwenberg B, von Lindern M (November 2000). "Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells". Blood 96 (10): 3406–13. PMID 11071635.
^ Yamanashi Y, Baltimore D (January 1997). "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok". Cell 88 (2): 205–11. doi:10.1016/S0092-8674(00)81841-3. PMID 9008161.
^ Yu HH, Zisch AH, Dodelet VC, Pasquale EB (July 2001). "Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor". Oncogene 20 (30): 3995–4006. doi:10.1038/sj.onc.1204524. PMID 11494128.
^ Cao C, Leng Y, Huang W, Liu X, Kufe D (October 2003). "Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases". J. Biol. Chem. 278 (41): 39609–14. doi:10.1074/jbc.M305770200. PMID 12893824.
^ Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY et al. (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene 17 (8): 941–8. doi:10.1038/sj.onc.1202024. PMID 9747873.
^ Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE (January 1997). "Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains". J. Biol. Chem. 272 (5): 2659–67. doi:10.1074/jbc.272.5.2659. PMID 9006901.
^ Kumar V, Sabatini D, Pandey P, Gingras AC, Majumder PK, Kumar M et al. (April 2000). "Regulation of the rapamycin and FKBP-target 1/mammalian target of rapamycin and cap-dependent initiation of translation by the c-Abl protein-tyrosine kinase". J. Biol. Chem. 275 (15): 10779–87. doi:10.1074/jbc.275.15.10779. PMID 10753870.
^ Warmuth M, Bergmann M, Priess A, Häuslmann K, Emmerich B, Hallek M (December 1997). "The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr". J. Biol. Chem. 272 (52): 33260–70. doi:10.1074/jbc.272.52.33260. PMID 9407116.
^ Goldberg Z, Vogt Sionov R, Berger M, Zwang Y, Perets R, Van Etten RA et al. (July 2002). "Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation". EMBO J. 21 (14): 3715–27. doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.
^ Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (October 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. 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.
^ Law SF, Estojak J, Wang B, Mysliwiec T, Kruh G, Golemis EA (July 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. 16 (7): 3327–37. PMC 231327. PMID 8668148.
^ Koch A, Mancini A, Stefan M, Niedenthal R, Niemann H, Tamura T (March 2000). "Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop". FEBS Lett. 469 (1): 72–6. doi:10.1016/S0014-5793(00)01242-4. PMID 10708759.
^ Yano H, Cong F, Birge RB, Goff SP, Chao MV (February 2000). "Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor". J. Neurosci. Res. 59 (3): 356–64. doi:10.1002/(SICI)1097-4547(20000201)59:3<356::AID-JNR9>3.0.CO;2-G. PMID 10679771.
^ Yuan ZM, Shioya H, Ishiko T, Sun X, Gu J, Huang YY et al. (June 1999). "p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage". Nature 399 (6738): 814–7. doi:10.1038/21704. PMID 10391251.
^ Agami R, Blandino G, Oren M, Shaul Y (June 1999). "Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis". Nature 399 (6738): 809–13. doi:10.1038/21697. PMID 10391250.
^ Wen ST, Van Etten RA (October 1997). "The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity". Genes Dev. 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.
^ Roig J, Tuazon PT, Zipfel PA, Pendergast AM, Traugh JA (December 2000). "Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14346–51. doi:10.1073/pnas.97.26.14346. PMC 18921. PMID 11121037.
^ Cong F, Spencer S, Côté JF, Wu Y, Tremblay ML, Lasky LA et al. (December 2000). "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation". Mol. Cell 6 (6): 1413–23. doi:10.1016/S1097-2765(00)00138-6. PMID 11163214.
^ Yoshida K, Komatsu K, Wang HG, Kufe D (May 2002). "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage". Mol. Cell. Biol. 22 (10): 3292–300. doi:10.1128/MCB.22.10.3292-3300.2002. PMC 133797. PMID 11971963.
^ Miyamura T, Nishimura J, Yufu Y, Nawata H (February 1997). "Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines". Int. J. Hematol. 65 (2): 115–21. doi:10.1016/S0925-5710(96)00539-7. PMID 9071815.
^ Welch PJ, Wang JY (November 1993). "A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle". Cell 75 (4): 779–90. doi:10.1016/0092-8674(93)90497-E. PMID 8242749.
^ Agami R, Shaul Y (April 1998). "The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes". Oncogene 16 (14): 1779–88. doi:10.1038/sj.onc.1201708. PMID 9583676.
^ Zhu J, Shore SK (December 1996). "c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein". Mol. Cell. Biol. 16 (12): 7054–62. PMC 231708. PMID 8943360.
^ Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM et al. (April 1999). "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells". Blood 93 (8): 2707–20. PMID 10194451.
^ Wang B, Golemis EA, Kruh GD (July 1997). "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". J. Biol. Chem. 272 (28): 17542–50. doi:10.1074/jbc.272.28.17542. PMID 9211900.
^ ^a ^b Ziemnicka-Kotula D, Xu J, Gu H, Potempska A, Kim KS, Jenkins EC et al. (May 1998). "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton". J. Biol. Chem. 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. PMID 9593709.
^ Bassermann F, Jahn T, Miething C, Seipel P, Bai RY, Coutinho S et al. (April 2002). "Association of Bcr-Abl with the proto-oncogene Vav is implicated in activation of the Rac-1 pathway". J. Biol. Chem. 277 (14): 12437–45. doi:10.1074/jbc.M112397200. PMID 11790798.
^ Rafalska I, Zhang Z, Benderska N, Wolff H, Hartmann AM, Brack-Werner R et al. (August 2004). "The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation". Hum. Mol. Genet. 13 (15): 1535–49. doi:10.1093/hmg/ddh167. PMID 15175272.
^ Bueno MJ, Pérez de Castro I, Gómez de Cedrón M, Santos J, Calin GA, Cigudosa JC et al. (June 2008). "Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression". Cancer Cell 13 (6): 496–506. doi:10.1016/j.ccr.2008.04.018. PMID 18538733.

External links

Genes, abl at the US National Library of Medicine Medical Subject Headings (MeSH)
Online 'Mendelian Inheritance in Man' (OMIM) 189980 (ABL)
Abelson Leukemia Virus at the US National Library of Medicine Medical Subject Headings (MeSH)
Drosophila Abl tyrosine kinase - The Interactive Fly
ABL1 Info with links in the Cell Migration Gateway
ABL1 on the Atlas of Genetics and Oncology

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. 慢性骨髄性白血病の分子遺伝学 molecular genetics of chronic myeloid leukemia
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. 急性骨髄性白血病の分子遺伝学 molecular genetics of acute myeloid leukemia
4. 本態性血小板血症の診断および臨床症状 diagnosis and clinical manifestations of essential thrombocythemia
5. 染色体の転座、欠失、および逆位 chromosomal translocations deletions and inversions

English Journal

Polyphenol tri-vanillic ester 13c inhibits P-JAK2V617F and Bcr-Abl oncokinase expression in correlation with STAT3/STAT5 inactivation and apoptosis induction in human leukemia cells.

Trécul A, Morceau F, Gaigneaux A, Orsini M, Chateauvieux S, Grandjenette C, Dicato M, Diederich M.SourceLaboratoire de Biologie Moléculaire et Cellulaire du Cancer, Hôpital Kirchberg, 9, Rue Edward Steichen, 2540 Luxembourg, Luxembourg.
Cancer letters.Cancer Lett.2013 Oct 28;340(1):30-42. doi: 10.1016/j.canlet.2013.06.023. Epub 2013 Jun 26.
Constitutive activity of kinases has been reported in many types of cancers, so that inhibition of "onco-kinases" became a validated anti-cancer strategy. We found that the polyphenol 13c, a tri-vanillate derivative, inhibited kinase phosphorylation in leukemia cells. P-JAK2, P-Src and P-PI3Kp85 inh
PMID 23811288

Antagonistic functional duality of cancer genes.

Stepanenko AA, Vassetzky YS, Kavsan VM.SourceState Key Laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo Street, Kyiv 03680, Ukraine. Electronic address: a.a.stepanenko@gmail.com.
Gene.Gene.2013 Oct 25;529(2):199-207. doi: 10.1016/j.gene.2013.07.047. Epub 2013 Aug 9.
Cancer evolution is a stochastic process both at the genome and gene levels. Most of tumors contain multiple genetic subclones, evolving in either succession or in parallel, either in a linear or branching manner, with heterogeneous genome and gene alterations, extensively rewired signaling networks
PMID 23933273

Apoptosis-antagonizing transcription factor (AATF) gene silencing: role in induction of apoptosis and down-regulation of estrogen receptor in breast cancer cells.

Sharma M.SourceDepartment of Biotechnology, Panjab University, Chandigarh, 160014, India, monika_sharma540@yahoo.com.
Biotechnology letters.Biotechnol Lett.2013 Oct;35(10):1561-70. doi: 10.1007/s10529-013-1257-8. Epub 2013 Jun 26.
Apoptosis-antagonizing transcription factor (AATF) is involved in transcriptional regulation, cell cycle control, DNA damage responses and in the execution of cell death programs. It also interacts directly with nuclear hormone receptors to enhance their transactivation. This study highlights the RN
PMID 23801113

Japanese Journal

急性リンパ性白血病の分子機構

玉井勇人,猪口孝一
臨床血液 56(3), 253-260, 2015
… 小児急性リンパ性白血病acute lymphoblastic leukemia (ALL)は過去数十年あまりの間に治療成績は飛躍的に向上し，約90%の患者が長期生存できるようになったが，MLL-AF4陽性ALLやbcr-abl陽性ALLの予後は未だ十分でない。 …
NAID 130005065343

Severe Case of Peripheral Leukocytosis Initially Diagnosed as Myelodysplastic Syndrome/Myeloproliferative Neoplasm, Unclassifiable, but Possibly Prefibrotic Primary Myelofibrosis

Ota Seisuke,Hiramatsu Yasushi,Kondo Eisei,Kasahara Akinori,Takada Saimon,Umena Sachio,Noguchi Toshio,Tanimoto Mitsune,Matsumura Tadashi
Acta Medica Okayama 68(6), 363-368, 2014-12
… A fluorescence in situ hybridization test could not detect the BCR-ABL fusion gene. …
NAID 120005525314

Molecular analysis of the BCR-ABL1 kinase domain in chronic-phase chronic myelogenous leukemia treated with tyrosine kinase inhibitors in practice: Study by the Nagasaki CML Study Group

Itonaga Hidehiro,Tsushima Hideki,Imanishi Daisuke,Hata Tomoko,Doi Yuko,Mori Sayaka,Sasaki Daisuke,Hasegawa Hiroo,Matsuo Emi,Nakashima Jun,Kato Takeharu,Horai Makiko,Taguchi Masataka,Matsuo Masatoshi,Taniguchi Hiroaki,Makiyama Junnya,Sato Shinya,Horio Kensuke,Ando Koji,Moriwaki Yuji,Sawayama Yasushi,Ogawa Daisuke,Yamasaki Reishi,Takasaki Yumi,Imaizumi Yoshitaka,Taguchi Jun,Kawaguchi Yasuhisa,Yoshida Shinichiro,Joh Tatsuro,Moriuchi Yukiyoshi,Nonaka Hiroaki,Soda Hisashi,Fukushima Takuya,Nagai Kazuhiro,Kamihira Shimeru,Tomonaga Masao,Yanagihara Katsunori,Miyazaki Yasushi
Leukemia Research 38(1), 76-83, 2014-01
… An appropriate trigger for BCR-ABL1 mutation analysis has not yet been established in unselected cohorts of chronic-phase chronic myelogenous leukemia patients. … Univariate analysis revealed that significant factors associated with not attaining a major molecular response (MMR) were the presence of the minor BCR-ABL1 fusion gene, a low daily dose of TKI, and the emergence of BCR-ABL1 kinase domain mutations conferring resistance to imatinib. …
NAID 120005367584

Related Pictures

★リンクテーブル★

リンク元	「abl遺伝子」
拡張検索	「c-abl gene」「v-abl gene」

「abl遺伝子」

ABL proto-oncogene 1, non-receptor tyrosine kinase
	PDB rendering based on 1ab2.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1AB2, 1ABL, 1AWO, 1BBZ, 1JU5, 1OPL, 1ZZP, 2ABL, 2E2B, 2F4J, 2FO0, 2G1T, 2G2F, 2G2H, 2G2I, 2GQG, 2HIW, 2HYY, 2HZ0, 2HZ4, 2HZI, 2O88, 2V7A, 3CS9, 3EG0, 3EG1, 3EG2, 3EG3, 3EGU, 3K2M, 3PYY, 3QRI, 3QRJ, 3QRK, 3T04, 3UE4, 3UYO, 4J9B, 4J9C, 4J9D, 4J9E, 4J9F, 4J9G, 4J9H, 4J9I, 4JJB, 4JJC, 4JJD, 4TWP, 4WA9, 4XEY
Identifiers
Symbols	ABL1 ; ABL; JTK7; bcr/abl; c-ABL; c-ABL1; p150; v-abl
External IDs	OMIM: 189980 MGI: 87859 HomoloGene: 3783 ChEMBL: 1862 GeneCards: ABL1 Gene
EC number	2.7.10.2
Gene ontology
Molecular function	• magnesium ion binding; • DNA binding; • actin monomer binding; • nicotinate-nucleotide adenylyltransferase activity; • protein kinase activity; • protein tyrosine kinase activity; • non-membrane spanning protein tyrosine kinase activity; • receptor binding; • protein binding; • ATP binding; • protein C-terminus binding; • SH3 domain binding; • syntaxin binding; • manganese ion binding; • actin filament binding; • mitogen-activated protein kinase binding; • proline-rich region binding;
Cellular component	• nucleus; • nucleoplasm; • nucleolus; • cytoplasm; • mitochondrion; • cytosol; • actin cytoskeleton; • extrinsic component of cytoplasmic side of plasma membrane; • cell leading edge; • nuclear membrane; • perinuclear region of cytoplasm;
Biological process	• B-1 B cell homeostasis; • positive regulation of protein phosphorylation; • B cell proliferation involved in immune response; • transitional one stage B cell differentiation; • mismatch repair; • regulation of transcription, DNA-templated; • cellular protein modification process; • autophagy; • cellular response to DNA damage stimulus; • DNA damage induced protein phosphorylation; • response to oxidative stress; • cell cycle arrest; • mitotic nuclear division; • epidermal growth factor receptor signaling pathway; • positive regulation of cytosolic calcium ion concentration; • small GTPase mediated signal transduction; • axon guidance; • blood coagulation; • intrinsic apoptotic signaling pathway in response to DNA damage; • regulation of autophagy; • cell migration; • peptidyl-tyrosine phosphorylation; • cerebellum morphogenesis; • negative regulation of cell-cell adhesion; • microspike assembly; • actin cytoskeleton organization; • regulation of endocytosis; • cell differentiation; • regulation of cell adhesion; • negative regulation of BMP signaling pathway; • positive regulation of osteoblast proliferation; • substrate adhesion-dependent cell spreading; • cellular response to oxidative stress; • peptidyl-tyrosine autophosphorylation; • Fc-gamma receptor signaling pathway involved in phagocytosis; • regulation of cell proliferation; • muscle cell differentiation; • signal transduction in response to DNA damage; • positive regulation of apoptotic process; • positive regulation of I-kappaB kinase/NF-kappaB signaling; • negative regulation of I-kappaB kinase/NF-kappaB signaling; • innate immune response; • negative regulation of mitotic cell cycle; • positive regulation of mitotic cell cycle; • alpha-beta T cell differentiation; • platelet-derived growth factor receptor signaling pathway; • spleen development; • thymus development; • collateral sprouting; • positive regulation of peptidyl-tyrosine phosphorylation; • activated T cell proliferation; • B cell receptor signaling pathway; • neuromuscular process controlling balance; • positive regulation of muscle cell differentiation; • positive regulation of release of sequestered calcium ion into cytosol; • positive regulation of oxidoreductase activity; • negative regulation of ubiquitin-protein transferase activity; • mitochondrial depolarization; • Bergmann glial cell differentiation; • negative regulation of ERK1 and ERK2 cascade; • positive regulation of ERK1 and ERK2 cascade; • cellular response to lipopolysaccharide; • negative regulation of protein serine/threonine kinase activity; • actin filament branching; • positive regulation of interleukin-2 secretion; • negative regulation of phospholipase C activity; • positive regulation of neuron death; • positive regulation of interferon-gamma secretion; • regulation of extracellular matrix organization; • cellular response to dopamine; • positive regulation of Wnt signaling pathway, planar cell polarity pathway; • regulation of cell motility; • regulation of actin cytoskeleton reorganization; • negative regulation of endothelial cell apoptotic process; • negative regulation of cellular senescence; • regulation of response to DNA damage stimulus;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

　　[★]

英: abl gene
関: c-abl遺伝子、v-abl癌遺伝子、abl癌遺伝子、c-abl癌原遺伝子、v-abl遺伝子

「c-abl gene」

　　[★]

c-abl遺伝子

関: abl gene、abl oncogene、c-abl proto-oncogene、v-abl gene、v-abl oncogene

「v-abl gene」

　　[★]

v-abl遺伝子

関: abl gene、abl oncogene、c-abl gene、c-abl proto-oncogene、v-abl oncogene

[pmid1857987-1] Szczylik C, Skorski T, Nicolaides NC, Manzella L, Malaguarnera L, Venturelli D et al. (August 1991). "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science 253 (5019): 562–5. doi:10.1126/science.1857987. PMID 1857987.

[2] "Entrez Gene: ABL1 v-abl Abelson murine leukemia viral oncogene homolog 1".

[pmid12672821-3] Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H et al. (June 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. doi:10.1074/jbc.M301447200. PMID 12672821.

[pmid9010225-4] Biesova Z, Piccoli C, Wong WT (January 1997). "Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth". Oncogene 14 (2): 233–41. doi:10.1038/sj.onc.1200822. PMID 9010225.

[pmid11418237-5] Yamamoto A, Suzuki T, Sakaki Y (June 2001). "Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease". Gene 271 (2): 159–69. doi:10.1016/S0378-1119(01)00521-2. PMID 11418237.

[pmid12569093-6] Cao C, Leng Y, Li C, Kufe D (April 2003). "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response". J. Biol. Chem. 278 (15): 12961–7. doi:10.1074/jbc.M300058200. PMID 12569093.

[pmid7590236-7] Dai Z, Pendergast AM (November 1995). "Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity". Genes Dev. 9 (21): 2569–82. doi:10.1101/gad.9.21.2569. PMID 7590236.

[pmid10212258-8] Chen G, Yuan SS, Liu W, Xu Y, Trujillo K, Song B et al. (April 1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". J. Biol. Chem. 274 (18): 12748–52. doi:10.1074/jbc.274.18.12748. PMID 10212258.

[pmid9168117-9] Shafman T, Khanna KK, Kedar P, Spring K, Kozlov S, Yen T et al. (May 1997). "Interaction between ATM protein and c-Abl in response to DNA damage". Nature 387 (6632): 520–3. doi:10.1038/387520a0. PMID 9168117.

[pmid11375976-10] Kishi S, Zhou XZ, Ziv Y, Khoo C, Hill DE, Shiloh Y et al. (August 2001). "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks". J. Biol. Chem. 276 (31): 29282–91. doi:10.1074/jbc.M011534200. PMID 11375976.

[pmid8810278-11] Salgia R, Pisick E, Sattler M, Li JL, Uemura N, Wong WK et al. (October 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.

[pmid7780740-12] Mayer BJ, Hirai H, Sakai R (March 1995). "Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases". Curr. Biol. 5 (3): 296–305. doi:10.1016/S0960-9822(95)00060-1. PMID 7780740.

[pmid8112292-13] Puil L, Liu J, Gish G, Mbamalu G, Bowtell D, Pelicci PG et al. (February 1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. 13 (4): 764–73. PMC 394874. PMID 8112292.

[pmid12543778-14] Ling X, Ma G, Sun T, Liu J, Arlinghaus RB (January 2003). "Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr". Cancer Res. 63 (2): 298–303. PMID 12543778.

[pmid1712671-15] Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON (July 1991). "BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner". Cell 66 (1): 161–71. doi:10.1016/0092-8674(91)90148-R. PMID 1712671.

[pmid12024016-16] Foray N, Marot D, Randrianarison V, Venezia ND, Picard D, Perricaudet M et al. (June 2002). "Constitutive association of BRCA1 and c-Abl and its ATM-dependent disruption after irradiation". Mol. Cell. Biol. 22 (12): 4020–32. doi:10.1128/MCB.22.12.4020-4032.2002. PMC 133860. PMID 12024016.

[pmid12777400-17] Cao C, Leng Y, Kufe D (August 2003). "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". J. Biol. Chem. 278 (32): 29667–75. doi:10.1074/jbc.M301292200. PMID 12777400.

[pmid11494134-18] Miyoshi-Akiyama T, Aleman LM, Smith JM, Adler CE, Mayer BJ (July 2001). "Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor". Oncogene 20 (30): 4058–69. doi:10.1038/sj.onc.1204528. PMID 11494134.

[pmid12475393-19] Soubeyran P, Barac A, Szymkiewicz I, Dikic I (February 2003). "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl". Biochem. J. 370 (Pt 1): 29–34. doi:10.1042/BJ20021539. PMC 1223168. PMID 12475393.

[pmid7926767-20] Ren R, Ye ZS, Baltimore D (April 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes Dev. 8 (7): 783–95. doi:10.1101/gad.8.7.783. PMID 7926767.

[pmid8978305-21] Heaney C, Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S et al. (January 1997). "Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation". Blood 89 (1): 297–306. PMID 8978305.

[pmid9820532-22] Kyono WT, de Jong R, Park RK, Liu Y, Heisterkamp N, Groffen J et al. (November 1998). "Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI)". J. Immunol. 161 (10): 5555–63. PMID 9820532.

[pmid11071635-23] van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Löwenberg B, von Lindern M (November 2000). "Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells". Blood 96 (10): 3406–13. PMID 11071635.

[pmid9008161-24] Yamanashi Y, Baltimore D (January 1997). "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok". Cell 88 (2): 205–11. doi:10.1016/S0092-8674(00)81841-3. PMID 9008161.

[pmid11494128-25] Yu HH, Zisch AH, Dodelet VC, Pasquale EB (July 2001). "Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor". Oncogene 20 (30): 3995–4006. doi:10.1038/sj.onc.1204524. PMID 11494128.

[pmid12893824-26] Cao C, Leng Y, Huang W, Liu X, Kufe D (October 2003). "Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases". J. Biol. Chem. 278 (41): 39609–14. doi:10.1074/jbc.M305770200. PMID 12893824.

[pmid9747873-27] Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY et al. (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene 17 (8): 941–8. doi:10.1038/sj.onc.1202024. PMID 9747873.

[pmid9006901-28] Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE (January 1997). "Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains". J. Biol. Chem. 272 (5): 2659–67. doi:10.1074/jbc.272.5.2659. PMID 9006901.

[pmid10753870-29] Kumar V, Sabatini D, Pandey P, Gingras AC, Majumder PK, Kumar M et al. (April 2000). "Regulation of the rapamycin and FKBP-target 1/mammalian target of rapamycin and cap-dependent initiation of translation by the c-Abl protein-tyrosine kinase". J. Biol. Chem. 275 (15): 10779–87. doi:10.1074/jbc.275.15.10779. PMID 10753870.

[pmid9407116-30] Warmuth M, Bergmann M, Priess A, Häuslmann K, Emmerich B, Hallek M (December 1997). "The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr". J. Biol. Chem. 272 (52): 33260–70. doi:10.1074/jbc.272.52.33260. PMID 9407116.

[pmid12110584-31] Goldberg Z, Vogt Sionov R, Berger M, Zwang Y, Perets R, Van Etten RA et al. (July 2002). "Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation". EMBO J. 21 (14): 3715–27. doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.

[pmid8879209-32] Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (October 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. 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.

[pmid8668148-33] Law SF, Estojak J, Wang B, Mysliwiec T, Kruh G, Golemis EA (July 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. 16 (7): 3327–37. PMC 231327. PMID 8668148.

[pmid10708759-34] Koch A, Mancini A, Stefan M, Niedenthal R, Niemann H, Tamura T (March 2000). "Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop". FEBS Lett. 469 (1): 72–6. doi:10.1016/S0014-5793(00)01242-4. PMID 10708759.

[pmid10679771-35] Yano H, Cong F, Birge RB, Goff SP, Chao MV (February 2000). "Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor". J. Neurosci. Res. 59 (3): 356–64. doi:10.1002/(SICI)1097-4547(20000201)59:3<356::AID-JNR9>3.0.CO;2-G. PMID 10679771.

[pmid10391251-36] Yuan ZM, Shioya H, Ishiko T, Sun X, Gu J, Huang YY et al. (June 1999). "p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage". Nature 399 (6738): 814–7. doi:10.1038/21704. PMID 10391251.

[pmid10391250-37] Agami R, Blandino G, Oren M, Shaul Y (June 1999). "Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis". Nature 399 (6738): 809–13. doi:10.1038/21697. PMID 10391250.

[pmid9334312-38] Wen ST, Van Etten RA (October 1997). "The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity". Genes Dev. 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.

[pmid11121037-39] Roig J, Tuazon PT, Zipfel PA, Pendergast AM, Traugh JA (December 2000). "Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14346–51. doi:10.1073/pnas.97.26.14346. PMC 18921. PMID 11121037.

[pmid11163214-40] Cong F, Spencer S, Côté JF, Wu Y, Tremblay ML, Lasky LA et al. (December 2000). "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation". Mol. Cell 6 (6): 1413–23. doi:10.1016/S1097-2765(00)00138-6. PMID 11163214.

[pmid11971963-41] Yoshida K, Komatsu K, Wang HG, Kufe D (May 2002). "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage". Mol. Cell. Biol. 22 (10): 3292–300. doi:10.1128/MCB.22.10.3292-3300.2002. PMC 133797. PMID 11971963.

[pmid9071815-42] Miyamura T, Nishimura J, Yufu Y, Nawata H (February 1997). "Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines". Int. J. Hematol. 65 (2): 115–21. doi:10.1016/S0925-5710(96)00539-7. PMID 9071815.

[pmid8242749-43] Welch PJ, Wang JY (November 1993). "A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle". Cell 75 (4): 779–90. doi:10.1016/0092-8674(93)90497-E. PMID 8242749.

[pmid9583676-44] Agami R, Shaul Y (April 1998). "The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes". Oncogene 16 (14): 1779–88. doi:10.1038/sj.onc.1201708. PMID 9583676.

[pmid8943360-45] Zhu J, Shore SK (December 1996). "c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein". Mol. Cell. Biol. 16 (12): 7054–62. PMC 231708. PMID 8943360.

[pmid10194451-46] Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM et al. (April 1999). "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells". Blood 93 (8): 2707–20. PMID 10194451.

[pmid9211900-47] Wang B, Golemis EA, Kruh GD (July 1997). "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". J. Biol. Chem. 272 (28): 17542–50. doi:10.1074/jbc.272.28.17542. PMID 9211900.

[pmid9593709-48] Ziemnicka-Kotula D, Xu J, Gu H, Potempska A, Kim KS, Jenkins EC et al. (May 1998). "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton". J. Biol. Chem. 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. PMID 9593709.

[pmid11790798-49] Bassermann F, Jahn T, Miething C, Seipel P, Bai RY, Coutinho S et al. (April 2002). "Association of Bcr-Abl with the proto-oncogene Vav is implicated in activation of the Rac-1 pathway". J. Biol. Chem. 277 (14): 12437–45. doi:10.1074/jbc.M112397200. PMID 11790798.

[pmid15175272-50] Rafalska I, Zhang Z, Benderska N, Wolff H, Hartmann AM, Brack-Werner R et al. (August 2004). "The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation". Hum. Mol. Genet. 13 (15): 1535–49. doi:10.1093/hmg/ddh167. PMID 15175272.

[pmid18538733-51] Bueno MJ, Pérez de Castro I, Gómez de Cedrón M, Santos J, Calin GA, Cigudosa JC et al. (June 2008). "Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression". Cancer Cell 13 (6): 496–506. doi:10.1016/j.ccr.2008.04.018. PMID 18538733.

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abl gene