BCL2L2
From Wikipedia, the free encyclopedia
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BCL2-like 2
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| PDB rendering based on 1mk3. | ||||||||||||||
| Available structures: 1mk3, 1o0l, 1zy3 | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | BCL2L2; BCL-W; BCLW; KIAA0271 | |||||||||||||
| External IDs | OMIM: 601931 MGI: 108052 HomoloGene: 2989 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 599 | 12050 | ||||||||||||
| Ensembl | ENSG00000129473 | ENSMUSG00000022194 | ||||||||||||
| Uniprot | Q92843 | P70345 | ||||||||||||
| Refseq | NM_004050 (mRNA) NP_004041 (protein) |
NM_007537 (mRNA) NP_031563 (protein) |
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| Location | Chr 14: 22.85 - 22.85 Mb | Chr 14: 53.84 - 53.84 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
BCL2-like 2, also known as BCL2L2, is a human gene.[1]
This gene encodes a member of the BCL-2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis.[1]
[edit] References
[edit] Further reading
- Gibson L, Holmgreen SP, Huang DC, et al. (1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival.". Oncogene 13 (4): 665–75. PMID 8761287.
- Nagase T, Seki N, Ishikawa K, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain.". DNA Res. 3 (5): 321–9, 341–54. PMID 9039502.
- O'Connor L, Strasser A, O'Reilly LA, et al. (1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis.". EMBO J. 17 (2): 384–95. doi:. PMID 9430630.
- Ross AJ, Waymire KG, Moss JE, et al. (1998). "Testicular degeneration in Bclw-deficient mice.". Nat. Genet. 18 (3): 251–6. doi:. PMID 9500547.
- Hsu SY, Lin P, Hsueh AJ (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. 12 (9): 1432–40. PMID 9731710.
- Middleton G, Wyatt S, Ninkina N, Davies AM (2001). "Reciprocal developmental changes in the roles of Bcl-w and Bcl-x(L) in regulating sensory neuron survival.". Development 128 (3): 447–57. PMID 11152643.
- O'Reilly LA, Print C, Hausmann G, et al. (2001). "Tissue expression and subcellular localization of the pro-survival molecule Bcl-w.". Cell Death Differ. 8 (5): 486–94. doi:. PMID 11423909.
- Bae J, Hsu SY, Leo CP, et al. (2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis.". Apoptosis 6 (5): 319–30. PMID 11483855.
- Puthalakath H, Villunger A, O'Reilly LA, et al. (2001). "Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis.". Science 293 (5536): 1829–32. doi:. PMID 11546872.
- Ayllón V, Cayla X, García A, et al. (2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad.". Eur. J. Immunol. 32 (7): 1847–55. doi:. PMID 12115603.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:. PMID 12477932.
- Denisov AY, Madiraju MS, Chen G, et al. (2003). "Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix.". J. Biol. Chem. 278 (23): 21124–8. doi:. PMID 12651847.
- Hinds MG, Lackmann M, Skea GL, et al. (2003). "The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity.". EMBO J. 22 (7): 1497–507. doi:. PMID 12660157.
- Wilson-Annan J, O'Reilly LA, Crawford SA, et al. (2003). "Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity.". J. Cell Biol. 162 (5): 877–87. doi:. PMID 12952938.
- Zhu X, Wang Y, Ogawa O, et al. (2004). "Neuroprotective properties of Bcl-w in Alzheimer disease.". J. Neurochem. 89 (5): 1233–40. doi:. PMID 15147516.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:. PMID 15489334.
- Chen L, Willis SN, Wei A, et al. (2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function.". Mol. Cell 17 (3): 393–403. doi:. PMID 15694340.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:. PMID 16344560.
- Denisov AY, Chen G, Sprules T, et al. (2006). "Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles.". Biochemistry 45 (7): 2250–6. doi:. PMID 16475813.
- Certo M, Del Gaizo Moore V, Nishino M, et al. (2006). "Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members.". Cancer Cell 9 (5): 351–65. doi:. PMID 16697956.

