Abelsonov mišji leukemijski viralni onkogen homolog 1 (ABL1) protein je koji je kod ljudi kodiran ABL1genom (raniji simbol ABL) lociranim na hromozomu 9.[1] c-Abl se ponekad koristi za imenovanje verzije gena prisutnog u genomu sisara, dok se v-Abl odnosi na viralni gen.
^Tani K; Sato Seiichi; Sukezane Taiko; Kojima Hiroshi; Hirose Hidenori; Hanafusa Hidesaburo; Shishido Tomoyuki (jun 2003). „Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase”. J. Biol. Chem. 278 (24): 21685—92. PMID12672821. doi:10.1074/jbc.M301447200.
^Biesova Z, Piccoli C, Wong WT (januar 1997). „Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth”. Oncogene. 14 (2): 233—41. PMID9010225. doi:10.1038/sj.onc.1200822.
^Yamamoto A, Suzuki T, Sakaki Y (jun 2001). „Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease”. Gene. 271 (2): 159—69. PMID11418237. doi:10.1016/S0378-1119(01)00521-2.
^ абCao 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. PMID12569093. doi:10.1074/jbc.M300058200.
^Dai Z, Pendergast AM (novembar 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. PMID7590236. doi:10.1101/gad.9.21.2569.
^ абChen G, Yuan SS, Liu W, Xu Y, Trujillo K, Song B, Cong F, Goff SP, Wu Y, Arlinghaus R, Baltimore D, Gasser PJ, Park MS, Sung P, Lee EY (april 1999). „Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl”. J. Biol. Chem. 274 (18): 12748—52. PMID10212258. doi:10.1074/jbc.274.18.12748.
^Shafman T, Khanna KK, Kedar P, Spring K, Kozlov S, Yen T, Hobson K, Gatei M, Zhang N, Watters D, Egerton M, Shiloh Y, Kharbanda S, Kufe D, Lavin MF (maj 1997). „Interaction between ATM protein and c-Abl in response to DNA damage”. Nature. 387 (6632): 520—3. PMID9168117. doi:10.1038/387520a0.
^ абKishi S, Zhou XZ, Ziv Y, Khoo C, Hill DE, Shiloh Y, Lu KP (avgust 2001). „Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks”. J. Biol. Chem. 276 (31): 29282—91. PMID11375976. doi:10.1074/jbc.M011534200.
^Salgia R, Pisick E, Sattler M, Li JL, Uemura N, Wong WK, Burky SA, Hirai H, Chen LB, Griffin JD (oktobar 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. PMID8810278. doi:10.1074/jbc.271.41.25198.
^Mayer BJ, Hirai H, Sakai R (mart 1995). „Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases”. Curr. Biol. 5 (3): 296—305. PMID7780740. doi:10.1016/S0960-9822(95)00060-1.
^Ling X; Ma Guozhen; Sun Tong; Liu Jiaxin; Arlinghaus Ralph B (januar 2003). „Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr”. Cancer Res. 63 (2): 298—303. PMID12543778.
^Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON (jul 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. PMID1712671. doi:10.1016/0092-8674(91)90148-R.
^Cao C; Leng Yumei; Kufe Donald (avgust 2003). „Catalase activity is regulated by c-Abl and Arg in the oxidative stress response”. J. Biol. Chem. 278 (32): 29667—75. PMID12777400. doi:10.1074/jbc.M301292200.
^ абMiyoshi-Akiyama T, Aleman LM, Smith JM, Adler CE, Mayer BJ (jul 2001). „Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor”. Oncogene. 20 (30): 4058—69. PMID11494134. doi:10.1038/sj.onc.1204528.
^ абвRen 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. PMID7926767. doi:10.1101/gad.8.7.783.
^Heaney C, Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S, Druker BJ (januar 1997). „Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation”. Blood. 89 (1): 297—306. PMID8978305.
^Kyono WT, de Jong R, Park RK, Liu Y, Heisterkamp N, Groffen J, Durden DL (novembar 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. PMID9820532.
^van Dijk TB; van Den Akker E; Amelsvoort M P; Mano H; Löwenberg B; von Lindern M (novembar 2000). „Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells”. Blood. 96 (10): 3406—13. PMID11071635.
^Yamanashi Y, Baltimore D (januar 1997). „Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok”. Cell. 88 (2): 205—11. PMID9008161. doi:10.1016/S0092-8674(00)81841-3.
^Yu HH, Zisch AH, Dodelet VC, Pasquale EB (jul 2001). „Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor”. Oncogene. 20 (30): 3995—4006. PMID11494128. doi:10.1038/sj.onc.1204524.
^Cao C; Leng Yumei; Huang Wei; Liu Xuan; Kufe Donald (oktobar 2003). „Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases”. J. Biol. Chem. 278 (41): 39609—14. PMID12893824. doi:10.1074/jbc.M305770200.
^Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (avgust 1998). „The SH2-containing adapter protein GRB10 interacts with BCR-ABL”. Oncogene. 17 (8): 941—8. PMID9747873. doi:10.1038/sj.onc.1202024.
^Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE (januar 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. PMID9006901. doi:10.1074/jbc.272.5.2659.
^Kumar V, Sabatini D, Pandey P, Gingras AC, Majumder PK, Kumar M, Yuan ZM, Carmichael G, Weichselbaum R, Sonenberg N, Kufe D, Kharbanda S (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. PMID10753870. doi:10.1074/jbc.275.15.10779.
^Warmuth M, Bergmann M, Priess A, Häuslmann K, Emmerich B, Hallek M (decembar 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. PMID9407116. doi:10.1074/jbc.272.52.33260.
^Koch A, Mancini A, Stefan M, Niedenthal R, Niemann H, Tamura T (mart 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. PMID10708759. doi:10.1016/S0014-5793(00)01242-4.
^Yuan ZM, Shioya H, Ishiko T, Sun X, Gu J, Huang YY, Lu H, Kharbanda S, Weichselbaum R, Kufe D (jun 1999). „p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage”. Nature. 399 (6738): 814—7. PMID10391251. doi:10.1038/21704.
^Agami R, Blandino G, Oren M, Shaul Y (jun 1999). „Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis”. Nature. 399 (6738): 809—13. PMID10391250. doi:10.1038/21697.
^Cong F, Spencer S, Côté JF, Wu Y, Tremblay ML, Lasky LA, Goff SP (decembar 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. PMID11163214. doi:10.1016/S1097-2765(00)00138-6.
^Miyamura T, Nishimura J, Yufu Y, Nawata H (februar 1997). „Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines”. Int. J. Hematol. 65 (2): 115—21. PMID9071815. doi:10.1016/S0925-5710(96)00539-7.
^Welch PJ, Wang JY (novembar 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. PMID8242749. doi:10.1016/0092-8674(93)90497-E.
^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. PMID9583676. doi:10.1038/sj.onc.1201708.
^Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B (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. PMID10194451.
^Wang B, Golemis EA, Kruh GD (jul 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. PMID9211900. doi:10.1074/jbc.272.28.17542.
^ абZiemnicka-Kotula D, Xu J, Gu H, Potempska A, Kim KS, Jenkins EC, Trenkner E, Kotula L (maj 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. PMID9593709. doi:10.1074/jbc.273.22.13681.
^Bassermann F, Jahn T, Miething C, Seipel P, Bai RY, Coutinho S, Tybulewicz VL, Peschel C, Duyster J (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. PMID11790798. doi:10.1074/jbc.M112397200.
^Rafalska I, Zhang Z, Benderska N, Wolff H, Hartmann AM, Brack-Werner R, Stamm S (avgust 2004). „The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation”. Hum. Mol. Genet. 13 (15): 1535—49. PMID15175272. doi:10.1093/hmg/ddh167.
^Bueno MJ, Pérez de Castro I, Gómez de Cedrón M, Santos J, Calin GA, Cigudosa JC, Croce CM, Fernández-Piqueras J, Malumbres M (jun 2008). „Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression”. Cancer Cell. 13 (6): 496—506. PMID18538733. doi:10.1016/j.ccr.2008.04.018.
Literatura
Shore SK, Tantravahi RV, Reddy EP (decembar 2002). „Transforming pathways activated by the v-Abl tyrosine kinase”. Oncogene. 21 (56): 8568—76. PMID12476303. doi:10.1038/sj.onc.1206084.
Era T (2002). „Bcr-Abl is a "molecular switch" for the decision for growth and differentiation in hematopoietic stem cells”. Int. J. Hematol. 76 (1): 35—43. PMID12138893. doi:10.1007/BF02982716.
Keung YK, Beaty M, Steward W, et al. (2003). „Chronic myelocytic leukemia with eosinophilia, t(9;12)(q34;p13), and ETV6-ABL gene rearrangement: case report and review of the literature”. Cancer Genet. Cytogenet. 138 (2): 139—42. PMID12505259. doi:10.1016/S0165-4608(02)00609-X.
Saglio G, Cilloni D (2005). „Abl: the prototype of oncogenic fusion proteins”. Cell. Mol. Life Sci. 61 (23): 2897—911. PMID15583852. doi:10.1007/s00018-004-4271-0.
Shaul Y, Ben-Yehoyada M (2005). „Role of c-Abl in the DNA damage stress response”. Cell Res. 15 (1): 33—5. PMID15686624. doi:10.1038/sj.cr.7290261.
Yoshida K (2007). „Regulation for nuclear targeting of the Abl tyrosine kinase in response to DNA damage”. Adv. Exp. Med. Biol. 604: 155—65. PMID17695727. doi:10.1007/978-0-387-69116-9_15.
Spoljašnje veze
Genes,+abl на US National Library of Medicine Medical Subject Headings (MeSH)