BCL2-like 1 (gene)
BCL2-like 1 |
PDB rendering based on 1af3. |
Available structures |
PDB |
1BXL, 1G5J, 1LXL, 1MAZ, 1R2D, 1R2E, 1R2G, 1R2H, 1R2I, 1YSG, 1YSI, 1YSN, 2B48, 2O1Y, 2O2M, 2O2N, 2P1L, 2PON, 2YXJ, 3CVA, 3FDL, 3FDM, 3INQ, 3IO8 |
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Identifiers |
Symbols |
BCL2L1; BCL-XL/S; BCL2L; BCLX; BCLXL; BCLXS; Bcl-X; DKFZp781P2092; bcl-xL; bcl-xS |
External IDs |
OMIM: 600039 MGI: 88139 HomoloGene: 7639 GeneCards: BCL2L1 Gene |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
598 |
12048 |
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Ensembl |
ENSG00000171552 |
ENSMUSG00000007659 |
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UniProt |
Q07817 |
Q3T9W4 |
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RefSeq (mRNA) |
NM_001191.2 |
NM_009743.4 |
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RefSeq (protein) |
NP_001182.1 |
NP_033873.3 |
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Location (UCSC) |
Chr 20:
30.25 – 30.31 Mb |
Chr 2:
152.59 – 152.66 Mb |
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PubMed search |
[1] |
[2] |
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Bcl-2-like protein 1 is a protein that in humans is encoded by the BCL2L1 gene.[1]
The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The proteins encoded by this gene are located at the outer mitochondrial membrane, and have been shown to regulate outer mitochondrial membrane channel (VDAC) opening. VDAC regulates mitochondrial membrane potential, and thus controls the production of reactive oxygen species(ROS) and release of cytochrome C by mitochondria, both of which are the potent inducers of cell apoptosis. Two alternatively spliced transcript variants, which encode distinct isoforms, have been reported. The longer isoform acts as an apoptotic inhibitor and the shorter form acts as an apoptotic activator.[2]
Interactions
BCL2-like 1 (gene) has been shown to interact with RAD9A,[3][4] RTN1,[5] BAK1,[3][6][7][8][9] Reticulon 4,[5] Bcl-2-associated X protein,[6][10][11] BCAP31,[12] Bcl-2-interacting killer,[3][11][13][14] PPP1CA,[15] Noxa,[13][16] VDAC1,[17][18][19][20] BCL2L11,[7][13][21][22] Bcl-2-associated death promoter,[4][6][10][13][15][23][24][25][26][27][28] Bcl-2,[6][29] BNIPL,[30][31] APAF1,[32][33] HRK,[7][34][35] IKZF3,[36] PSEN2[37] and BNIP3.[38]
References
- ^ Boise LH, Gonzalez-Garcia M, Postema CE, Ding L, Lindsten T, Turka LA, Mao X, Nunez G, Thompson CB (Sep 1993). "bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death". Cell 74 (4): 597–608. doi:10.1016/0092-8674(93)90508-N. PMID 8358789.
- ^ "Entrez Gene: BCL2L1 BCL2-like 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=598.
- ^ a b c Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ^ a b Komatsu, K; Miyashita T, Hang H, Hopkins K M, Zheng W, Cuddeback S, Yamada M, Lieberman H B, Wang H G (Jan. 2000). "Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis". Nat. Cell Biol. (ENGLAND) 2 (1): 1–6. doi:10.1038/71316. ISSN 1465-7392. PMID 10620799.
- ^ a b Tagami, S; Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (Nov. 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. doi:10.1038/sj.onc.1203948. ISSN 0950-9232. PMID 11126360.
- ^ a b c d Zhang, Haichao; Nimmer Paul, Rosenberg Saul H, Ng Shi-Chung, Joseph Mary (Aug. 2002). "Development of a high-throughput fluorescence polarization assay for Bcl-x(L)". Anal. Biochem. (United States) 307 (1): 70–5. doi:10.1016/S0003-2697(02)00028-3. ISSN 0003-2697. PMID 12137781.
- ^ a b c Whitfield, Jonathan; Harada Kokichi, Bardelle Catherine, Staddon James M (Nov. 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Anal. Biochem. (United States) 322 (2): 170–8. doi:10.1016/j.ab.2003.07.014. ISSN 0003-2697. PMID 14596824.
- ^ Willis, Simon N; Chen Lin, Dewson Grant, Wei Andrew, Naik Edwina, Fletcher Jamie I, Adams Jerry M, Huang David C S (Jun. 2005). "Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins". Genes Dev. (United States) 19 (11): 1294–305. doi:10.1101/gad.1304105. ISSN 0890-9369. PMC 1142553. PMID 15901672. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1142553.
- ^ Degterev, A; Lugovskoy A, Cardone M, Mulley B, Wagner G, Mitchison T, Yuan J (Feb. 2001). "Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL". Nat. Cell Biol. (England) 3 (2): 173–82. doi:10.1038/35055085. ISSN 1465-7392. PMID 11175750.
- ^ a b Strobel, T; Tai Y T, Korsmeyer S, Cannistra S A (Nov. 1998). "BAD partly reverses paclitaxel resistance in human ovarian cancer cells". Oncogene (ENGLAND) 17 (19): 2419–27. doi:10.1038/sj.onc.1202180. ISSN 0950-9232. PMID 9824152.
- ^ a b Gillissen, Bernhard; Essmann Frank, Graupner Vilma, Stärck Lilian, Radetzki Silke, Dörken Bernd, Schulze-Osthoff Klaus, Daniel Peter T (Jul. 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. doi:10.1093/emboj/cdg343. ISSN 0261-4189. PMC 165613. PMID 12853473. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=165613.
- ^ Ng, F W; Nguyen M, Kwan T, Branton P E, Nicholson D W, Cromlish J A, Shore G C (Oct. 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. doi:10.1083/jcb.139.2.327. ISSN 0021-9525. PMC 2139787. PMID 9334338. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2139787.
- ^ a b c d Chen, Lin; Willis Simon N, Wei Andrew, Smith Brian J, Fletcher Jamie I, Hinds Mark G, Colman Peter M, Day Catherine L, Adams Jerry M, Huang David C S (Feb. 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. doi:10.1016/j.molcel.2004.12.030. ISSN 1097-2765. PMID 15694340.
- ^ Jiang, A; Clark E A (May. 2001). "Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis". J. Immunol. (United States) 166 (10): 6025–33. ISSN 0022-1767. PMID 11342619.
- ^ a b Ayllón, Verónica; Cayla Xavier, García Alphonse, Fleischer Aarne, Rebollo Angelita (Jul. 2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad". Eur. J. Immunol. (Germany) 32 (7): 1847–55. doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. ISSN 0014-2980. PMID 12115603.
- ^ Oda, E; Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (May. 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. doi:10.1126/science.288.5468.1053. ISSN 0036-8075. PMID 10807576.
- ^ Weng, Changjiang; Li Yuan, Xu Dan, Shi Yong, Tang Hong (Mar. 2005). "Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells". J. Biol. Chem. (United States) 280 (11): 10491–500. doi:10.1074/jbc.M412819200. ISSN 0021-9258. PMID 15637055.
- ^ Shi, Yong; Chen Jianjun, Weng Changjiang, Chen Rui, Zheng Yanhua, Chen Quan, Tang Hong (Jun. 2003). "Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins". Biochem. Biophys. Res. Commun. (United States) 305 (4): 989–96. doi:10.1016/S0006-291X(03)00871-4. ISSN 0006-291X. PMID 12767928.
- ^ Shimizu, S; Konishi A, Kodama T, Tsujimoto Y (Mar. 2000). "BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (7): 3100–5. doi:10.1073/pnas.97.7.3100. ISSN 0027-8424. PMC 16199. PMID 10737788. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16199.
- ^ Shimizu, S; Narita M, Tsujimoto Y (Jun. 1999). "Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC". Nature (ENGLAND) 399 (6735): 483–7. doi:10.1038/20959. ISSN 0028-0836. PMID 10365962.
- ^ O'Connor, L; Strasser A, O'Reilly L A, Hausmann G, Adams J M, Cory S, Huang D C (Jan. 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. (ENGLAND) 17 (2): 384–95. doi:10.1093/emboj/17.2.384. ISSN 0261-4189. PMC 1170389. PMID 9430630. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170389.
- ^ Hsu, S Y; Lin P, Hsueh A J (Sep. 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. doi:10.1210/me.12.9.1432. ISSN 0888-8809. PMID 9731710.
- ^ Jin, Zhaohui; Xin Meiguo, Deng Xingming (Apr. 2005). "Survival function of protein kinase C{iota} as a novel nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-activated bad kinase". J. Biol. Chem. (United States) 280 (16): 16045–52. doi:10.1074/jbc.M413488200. ISSN 0021-9258. PMID 15705582.
- ^ Yang, E; Zha J, Jockel J, Boise L H, Thompson C B, Korsmeyer S J (Jan. 1995). "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death". Cell (UNITED STATES) 80 (2): 285–91. doi:10.1016/0092-8674(95)90411-5. ISSN 0092-8674. PMID 7834748.
- ^ Petros, A M; Nettesheim D G, Wang Y, Olejniczak E T, Meadows R P, Mack J, Swift K, Matayoshi E D, Zhang H, Thompson C B, Fesik S W (Dec. 2000). "Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies". Protein Sci. (United States) 9 (12): 2528–34. doi:10.1110/ps.9.12.2528. ISSN 0961-8368. PMC 2144516. PMID 11206074. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2144516.
- ^ Chattopadhyay, A; Chiang C W, Yang E (Jul. 2001). "BAD/BCL-[X(L)] heterodimerization leads to bypass of G0/G1 arrest". Oncogene (England) 20 (33): 4507–18. doi:10.1038/sj.onc.1204584. ISSN 0950-9232. PMID 11494146.
- ^ Iwahashi, H; Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (Nov. 1997). "Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy". Nature (ENGLAND) 390 (6658): 413–7. doi:10.1038/37144. ISSN 0028-0836. PMID 9389483.
- ^ Komatsu, K; Wharton W, Hang H, Wu C, Singh S, Lieberman H B, Pledger W J, Wang H G (Nov. 2000). "PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition". Oncogene (ENGLAND) 19 (46): 5291–7. doi:10.1038/sj.onc.1203901. ISSN 0950-9232. PMID 11077446.
- ^ Lin, Bingzhen; Kolluri Siva Kumar, Lin Feng, Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun (Feb. 2004). "Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3". Cell (United States) 116 (4): 527–40. doi:10.1016/S0092-8674(04)00162-X. ISSN 0092-8674. PMID 14980220.
- ^ Qin, Wenxin; Hu Jian, Guo Minglei, Xu Jian, Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren (Aug. 2003). "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. doi:10.1016/S0006-291X(03)01387-1. ISSN 0006-291X. PMID 12901880.
- ^ Yasuda, M; Han J W, Dionne C A, Boyd J M, Chinnadurai G (Feb. 1999). "BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3". Cancer Res. (UNITED STATES) 59 (3): 533–7. ISSN 0008-5472. PMID 9973195.
- ^ Hu, Y; Benedict M A, Wu D, Inohara N, Núñez G (Apr. 1998). "Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (8): 4386–91. doi:10.1073/pnas.95.8.4386. ISSN 0027-8424. PMC 22498. PMID 9539746. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22498.
- ^ Pan, G; O'Rourke K, Dixit V M (Mar. 1998). "Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex". J. Biol. Chem. (UNITED STATES) 273 (10): 5841–5. doi:10.1074/jbc.273.10.5841. ISSN 0021-9258. PMID 9488720.
- ^ Inohara, N; Ding L, Chen S, Núñez G (Apr. 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. doi:10.1093/emboj/16.7.1686. ISSN 0261-4189. PMC 1169772. PMID 9130713. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169772.
- ^ Imaizumi, K; Morihara T, Mori Y, Katayama T, Tsuda M, Furuyama T, Wanaka A, Takeda M, Tohyama M (Mar. 1999). "The cell death-promoting gene DP5, which interacts with the BCL2 family, is induced during neuronal apoptosis following exposure to amyloid beta protein". J. Biol. Chem. (UNITED STATES) 274 (12): 7975–81. doi:10.1074/jbc.274.12.7975. ISSN 0021-9258. PMID 10075695.
- ^ Rebollo, A; Ayllón V, Fleischer A, Martínez C A, Zaballos A (Dec. 2001). "The association of Aiolos transcription factor and Bcl-xL is involved in the control of apoptosis". J. Immunol. (United States) 167 (11): 6366–73. ISSN 0022-1767. PMID 11714801.
- ^ Passer, B J; Pellegrini L, Vito P, Ganjei J K, D'Adamio L (Aug. 1999). "Interaction of Alzheimer's presenilin-1 and presenilin-2 with Bcl-X(L). A potential role in modulating the threshold of cell death". J. Biol. Chem. (UNITED STATES) 274 (34): 24007–13. doi:10.1074/jbc.274.34.24007. ISSN 0021-9258. PMID 10446169.
- ^ Ray, R; Chen G, Vande Velde C, Cizeau J, Park J H, Reed J C, Gietz R D, Greenberg A H (Jan. 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. doi:10.1074/jbc.275.2.1439. ISSN 0021-9258. PMID 10625696.
Further reading
PDB gallery
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1af3: RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN
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1bxl: STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE
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1lxl: NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE
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1maz: X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH
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1pq0: Crystal structure of mouse Bcl-xl
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1pq1: Crystal structure of Bcl-xl/Bim
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1r2d: Structure of Human Bcl-XL at 1.95 Angstroms
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1r2e: Human Bcl-XL containing a Glu to Leu mutation at position 92
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1r2g: Human Bcl-XL containing a Phe to Trp mutation at position 97
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1r2h: Human Bcl-XL containing an Ala to Leu mutation at position 142
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1r2i: Human Bcl-XL containing a Phe to Leu mutation at position 146
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2b48: Bcl-XL 3D Domain Swapped Dimer
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2bzw: THE CRYSTAL STRUCTURE OF BCL-XL IN COMPLEX WITH FULL-LENGTH BAD
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