Википедија

Bcl-2

(преусмерено са BCL2)

Bcl-2 (B-ćelijski limfom 2) je član Bcl-2 familije proteinskih regulatora apoptoze. On je kodiran BCL2 genom.[1][2] Bcl-2 je drugi član niza proteina koji su inicijalno bili opisani u kontekstu hromozomske translokacije hromozoma 14 i 18 kod folikularnih limfoma. Bcl-2 ortolozi[3] postoje kod mnogobrojnih sisara. Dve izoforme Bcl-2, Izoforma 1, takođe poznata kao 1G5M, i Izoforma 2, poznata kao 1G5O/1GJH, imaju sličnu prostornu strukturu. Međutim, one se razlikuju u njihovoj sposobnosti vezivanja BAD u BAK proteina, kao i po strukturnoj topologiji i elektrostatičkom potencijalu vezujućeg žljeba. Iz toga sledi da Bcl-2 izoforme imaju različite antiapoptotičke aktivnosti.[4]

B-ćelijski CLL/limfom 2
PDB prikaz bazairan na 1GJH​, 1G5M​.
Dostupne strukture
1G5M​, 1GJH​, 1YSW​, 2O21​, 2O22​, 2O2F​, 2W3L​, 2XA0​
Identifikatori
Simboli BCL2; Bcl-2; PPP1R50
Vanjski ID OMIM: 151430 MGI: 88138 HomoloGene: 527 GeneCards: BCL2 Gene
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 596 12043
Ensembl ENSG00000171791 ENSMUSG00000057329
UniProt P10415 Q4VBF6
RefSeq (mRNA) NM_000633.2 NM_009741.3
RefSeq (protein) NP_000624.2 NP_033871.2
Lokacija (UCSC) Chr 18:
60.79 - 60.99 Mb		 Chr 1:
108.43 - 108.61 Mb
PubMed pretraga [1] [2]

Interakcije уреди

Bcl-2 formira interakcije sa RAD9A,[5] BAK1,[6][7] Retikulon 4,[8] Bcl-2 asocirani X protein,[5][6][9][10] Kaspaza 8,[11][12] BECN1,[13] SOD1,[14] Bcl-2 interagujući ubica,[15][16] BH3 interagujući domen agonista umiranja,[15][17] RRAS,[18] C-Raf,[19] BCL2L11,[15][20][21] BNIPL,[22][23] HRK,[15][24] PSEN1,[25] BMF,[26] BNIP2,[22][27] BNIP3,[27][28] Faktor rasta nerva IB,[6] BCL2-sličan 1,[6][29] Myc,[30] BCAP31,[31] SMN1,[32] CAPN2,[33] PPP2CA,[34] Noxa,[15][35] Cdk1,[36][37] TP53BP2,[38] Bcl-2 vezan promoter smrti[15][39] i IRS1.[40]

Ljudski BCL-2 geni уреди

BAK, BAK1, BAX, BCL2, BCL2A1, BCL2L1, BCL2L10, BCL2L13, BCL2L14, BCL2L2,BCL2L7P1, BOK, MCL1, LGALS7 (Galektin-7)

Reference уреди

  1. ^ Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM (1984). „Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation”. Science. 226 (4678): 1097—99. PMID 6093263. doi:10.1126/science.6093263. 
  2. ^ Cleary ML, Smith SD, Sklar J (1986). „Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation”. Cell. 47 (1): 19—28. PMID 2875799. doi:10.1016/0092-8674(86)90362-4. 
  3. ^ „OrthoMaM phylogenetic marker: Bcl-2 coding sequence”. Архивирано из оригинала 24. 09. 2015. г. Приступљено 13. 05. 2012. 
  4. ^ „Human Bcl2, Isoform 1”. 
  5. ^ а б Komatsu K, Miyashita T, Hang H, Hopkins KM, Zheng W, Cuddeback S, Yamada M, Lieberman HB, Wang HG (2000). „Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. ENGLAND. 2 (1): 1—6. ISSN 1465-7392. PMID 10620799. doi:10.1038/71316. 
  6. ^ а б в г Lin, Bingzhen; Kolluri Siva Kumar; Lin Feng (2004). Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun. „Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell. United States. 116 (4): 527—40. ISSN 0092-8674. PMID 14980220. doi:10.1016/S0092-8674(04)00162-X. 
  7. ^ Enyedy IJ, Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, Guo R, Li B, Zhu X, Huang Y, Long YQ, Roller PP, Yang D, Wang S (2001). „Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. J. Med. Chem. United States. 44 (25): 4313—24. ISSN 0022-2623. PMID 11728179. doi:10.1021/jm010016f. 
  8. ^ Tagami S, Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (2000). „A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene. England. 19 (50): 5736—46. ISSN 0950-9232. PMID 11126360. doi:10.1038/sj.onc.1203948. 
  9. ^ Hoetelmans, R W M (2004). „Nuclear partners of Bcl-2: Bax and PML”. DNA Cell Biol. United States. 23 (6): 351—4. ISSN 1044-5498. PMID 15231068. doi:10.1089/104454904323145236. 
  10. ^ Oltvai, Z N; Milliman C L; Korsmeyer S J (1993). „Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell. UNITED STATES. 74 (4): 609—19. ISSN 0092-8674. PMID 8358790. doi:10.1016/0092-8674(93)90509-O. 
  11. ^ Poulaki V, Mitsiades N, Romero ME, Tsokos M (2001). „Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2”. Cancer Res. United States. 61 (12): 4864—72. ISSN 0008-5472. PMID 11406564. 
  12. ^ Guo, Yin; Srinivasula Srinivasa M; Druilhe Anne; Fernandes-Alnemri Teresa; Alnemri Emad S (2002). „Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. J. Biol. Chem. United States. 277 (16): 13430—7. ISSN 0021-9258. PMID 11832478. doi:10.1074/jbc.M108029200. 
  13. ^ Liang XH, Kleeman LK, Jiang HH, Gordon G, Goldman JE, Berry G, Herman B, Levine B (1998). „Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein”. J. Virol. UNITED STATES. 72 (11): 8586—96. ISSN 0022-538X. PMC 110269  . PMID 9765397. 
  14. ^ Pasinelli, Piera; Belford Mary Elizabeth; Lennon Niall; Bacskai Brian J; Hyman Bradley T; Trotti Davide; Brown Robert H (2004). „Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria”. Neuron. United States. 43 (1): 19—30. ISSN 0896-6273. PMID 15233914. doi:10.1016/j.neuron.2004.06.021. 
  15. ^ а б в г д ђ Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (2005). „Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell. United States. 17 (3): 393—403. ISSN 1097-2765. PMID 15694340. doi:10.1016/j.molcel.2004.12.030. 
  16. ^ Gillissen, Bernhard; Essmann Frank; Graupner Vilma; Stärck Lilian; Radetzki Silke; Dörken Bernd; Schulze-Osthoff Klaus; Daniel Peter T (2003). „Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway”. EMBO J. England. 22 (14): 3580—90. ISSN 0261-4189. PMC 165613  . PMID 12853473. doi:10.1093/emboj/cdg343. 
  17. ^ Real, Pedro Jose; Cao Yeyu; Wang Renxiao; Nikolovska-Coleska Zaneta (2004). Sanz-Ortiz Jaime, Wang Shaomeng, Fernandez-Luna Jose Luis. „Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Res. United States. 64 (21): 7947—53. ISSN 0008-5472. PMID 15520201. doi:10.1158/0008-5472.CAN-04-0945. 
  18. ^ Fernandez-Sarabia, M J; Bischoff J R (1993). „Bcl-2 associates with the ras-related protein R-ras p23”. Nature. ENGLAND. 366 (6452): 274—5. ISSN 0028-0836. PMID 8232588. doi:10.1038/366274a0. 
  19. ^ Wang, H G; Rapp U R; Reed J C (1996). „Bcl-2 targets the protein kinase Raf-1 to mitochondria”. Cell. UNITED STATES. 87 (4): 629—38. ISSN 0092-8674. PMID 8929532. doi:10.1016/S0092-8674(00)81383-5. 
  20. ^ O'Connor, L; Strasser A; O'Reilly L A; Hausmann G; Adams J M; Cory S; Huang D C (1998). „Bim: a novel member of the Bcl-2 family that promotes apoptosis”. EMBO J. ENGLAND. 17 (2): 384—95. ISSN 0261-4189. PMC 1170389  . PMID 9430630. doi:10.1093/emboj/17.2.384. 
  21. ^ Hsu, S Y; Lin P; Hsueh A J (1998). „BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members”. Mol. Endocrinol. UNITED STATES. 12 (9): 1432—40. ISSN 0888-8809. PMID 9731710. doi:10.1210/me.12.9.1432. 
  22. ^ а б Qin, Wenxin; Hu Jian; Guo Minglei; Xu Jian (2003). Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren. „BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis”. Biochem. Biophys. Res. Commun. United States. 308 (2): 379—85. ISSN 0006-291X. PMID 12901880. doi:10.1016/S0006-291X(03)01387-1. 
  23. ^ Yasuda, M; Han J W; Dionne C A; Boyd J M; Chinnadurai G (1999). „BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3”. Cancer Res. UNITED STATES. 59 (3): 533—7. ISSN 0008-5472. PMID 9973195. 
  24. ^ Inohara, N; Ding L; Chen S; Núñez G (1997). „harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)”. EMBO J. ENGLAND. 16 (7): 1686—94. ISSN 0261-4189. PMC 1169772  . PMID 9130713. doi:10.1093/emboj/16.7.1686. 
  25. ^ Alberici A, Moratto D, Benussi L, Gasparini L, Ghidoni R, Gatta LB, Finazzi D, Frisoni GB, Trabucchi M, Growdon JH, Nitsch RM, Binetti G (1999). „Presenilin 1 protein directly interacts with Bcl-2”. J. Biol. Chem. UNITED STATES. 274 (43): 30764—9. ISSN 0021-9258. PMID 10521466. doi:10.1074/jbc.274.43.30764. 
  26. ^ Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A (2001). „Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science. United States. 293 (5536): 1829—32. ISSN 0036-8075. PMID 11546872. doi:10.1126/science.1062257. 
  27. ^ а б Boyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (1994). „Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell. UNITED STATES. 79 (2): 341—51. ISSN 0092-8674. PMID 7954800. doi:10.1016/0092-8674(94)90202-X. 
  28. ^ Ray R, Chen G, Vande VC, Cizeau J, Park JH, Reed JC, Gietz RD, Greenberg AH (2000). „BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites”. J. Biol. Chem. UNITED STATES. 275 (2): 1439—48. ISSN 0021-9258. PMID 10625696. doi:10.1074/jbc.275.2.1439. 
  29. ^ Zhang, Haichao; Nimmer Paul; Rosenberg Saul H; Ng Shi-Chung; Joseph Mary (2002). „Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. United States. 307 (1): 70—5. ISSN 0003-2697. PMID 12137781. doi:10.1016/S0003-2697(02)00028-3. 
  30. ^ Jin, Zhaohui; Gao Fengqin; Flagg Tammy; Deng Xingming (2004). „Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. United States. 279 (38): 40209—19. ISSN 0021-9258. PMID 15210690. doi:10.1074/jbc.M404056200. 
  31. ^ Ng FW, Nguyen M, Kwan T, Branton PE, Nicholson DW, Cromlish JA, Shore GC (1997). „p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum”. J. Cell Biol. UNITED STATES. 139 (2): 327—38. ISSN 0021-9525. PMC 2139787  . PMID 9334338. doi:10.1083/jcb.139.2.327. 
  32. ^ Iwahashi H, Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (1997). „Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature. ENGLAND. 390 (6658): 413—7. ISSN 0028-0836. PMID 9389483. doi:10.1038/37144. 
  33. ^ Gil-Parrado, Shirley; Fernández-Montalván Amaury; Assfalg-Machleidt Irmgard; Popp Oliver; Bestvater Felix (2002). Holloschi Andreas, Knoch Tobias A, Auerswald Ennes A, Welsh Katherine, Reed John C, Fritz Hans, Fuentes-Prior Pablo, Spiess Eberhard, Salvesen Guy S, Machleidt Werner. „Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. J. Biol. Chem. United States. 277 (30): 27217—26. ISSN 0021-9258. PMID 12000759. doi:10.1074/jbc.M202945200. 
  34. ^ Deng X, Ito T, Carr B, Mumby M, May WS (1998). „Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. J. Biol. Chem. UNITED STATES. 273 (51): 34157—63. ISSN 0021-9258. PMID 9852076. doi:10.1074/jbc.273.51.34157. 
  35. ^ Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (2000). „Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science. UNITED STATES. 288 (5468): 1053—8. ISSN 0036-8075. PMID 10807576. doi:10.1126/science.288.5468.1053. 
  36. ^ Pathan N, Aime-Sempe C, Kitada S, Basu A, Haldar S, Reed JC (2001). „Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1”. Neoplasia. United States. 3 (6): 550—9. ISSN 1522-8002. PMC 1506558  . PMID 11774038. doi:10.1038/sj/neo/7900213. 
  37. ^ Pathan N, Aime-Sempe C, Kitada S, Haldar S, Reed JC (2001). „Microtubule-targeting drugs induce Bcl-2 phosphorylation and association with Pin1”. Neoplasia. United States. 3 (1): 70—9. ISSN 1522-8002. PMC 1505024  . PMID 11326318. doi:10.1038/sj/neo/7900131. 
  38. ^ Naumovski, L; Cleary M L (1996). „The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M”. Mol. Cell. Biol. UNITED STATES. 16 (7): 3884—92. ISSN 0270-7306. PMC 231385  . PMID 8668206. 
  39. ^ Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ (1995). „Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death”. Cell. UNITED STATES. 80 (2): 285—91. ISSN 0092-8674. PMID 7834748. doi:10.1016/0092-8674(95)90411-5. 
  40. ^ Ueno H, Kondo E, Yamamoto-Honda R, Tobe K, Nakamoto T, Sasaki K, Mitani K, Furusaka A, Tanaka T, Tsujimoto Y, Kadowaki T, Hirai H (2000). „Association of insulin receptor substrate proteins with Bcl-2 and their effects on its phosphorylation and antiapoptotic function”. Mol. Biol. Cell. UNITED STATES. 11 (2): 735—46. ISSN 1059-1524. PMC 14806  . PMID 10679027. 

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