BMF (gene)

Bcl2 modifying factor
Identifiers
Symbols	BMF ; FLJ00065
External IDs	OMIM: 606266 MGI: 2176433 HomoloGene: 14130 GeneCards: BMF Gene
Gene ontology Molecular function • protein binding Cellular component • acrosomal vesicle • mitochondrial outer membrane • cytosol • plasma membrane • myosin complex Biological process • apoptotic process • programmed cell death • positive regulation of protein homooligomerization • anoikis • positive regulation of release of cytochrome c from mitochondria • intrinsic apoptotic signaling pathway • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway • negative regulation of apoptotic signaling pathway • positive regulation of intrinsic apoptotic signaling pathway Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	90427	171543
Ensembl	ENSG00000104081	ENSMUSG00000040093
UniProt	Q96LC9	Q91ZE9
RefSeq (mRNA)	NM_001003940	NM_138313
RefSeq (protein)	NP_001003940	NP_612186
Location (UCSC)	Chr 15: 40.09 – 40.11 Mb	Chr 2: 118.53 – 118.55 Mb
PubMed search

Bcl-2-modifying factor is a protein that in humans is encoded by the BMF gene.^[1][2]

The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. This protein is found to be sequestered to myosin V motors by its association with dynein light chain 2, which may be important for sensing intracellular damage and triggering apoptosis. Alternatively spliced transcript variants encoding different isoforms have been identified.^[2]

Interactions

BMF (gene) has been shown to interact with Bcl-2^[1] and DYNLL2.^[1][3]

References

1. Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A (Sep 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:10.1126/science.1062257. PMID 11546872.
2. "Entrez Gene: BMF Bcl2 modifying factor".
3. Day, Catherine L; Puthalakath Hamsa; Skea Gretchen; Strasser Andreas; Barsukov Igor; Lian Lu-Yun; Huang David C S; Hinds Mark G (Feb 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. (England) 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.

Further reading

• Hattori A, Okumura K, Nagase T; et al. (2001). "Characterization of long cDNA clones from human adult spleen.". DNA Res. 7 (6): 357–66. doi:10.1093/dnares/7.6.357. PMID 11214971.
• 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:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Lei K, Davis RJ (2003). "JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis.". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2432–7. doi:10.1073/pnas.0438011100. PMC 151358. PMID 12591950.
• Day CL, Puthalakath H, Skea G; et al. (2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.". Biochem. J. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.
• Morales AA, Olsson A, Celsing F; et al. (2004). "Expression and transcriptional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells.". Leukemia 18 (1): 41–7. doi:10.1038/sj.leu.2403183. PMID 14574334.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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:10.1101/gr.2596504. PMC 528928. 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:10.1016/j.molcel.2004.12.030. PMID 15694340.
• Kuwana T, Bouchier-Hayes L, Chipuk JE; et al. (2005). "BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly.". Mol. Cell 17 (4): 525–35. doi:10.1016/j.molcel.2005.02.003. PMID 15721256.
• Soung YH, Lee JW, Park WS; et al. (2006). "BH3 domain mutation of proapoptotic genes Bad, Bmf and Bcl-G is rare in transitional cell carcinomas of the urinary bladder.". Pathology 38 (1): 33–4. doi:10.1080/00313020500455811. PMID 16484005.
• Zhang Y, Adachi M, Kawamura R; et al. (2007). "Bmf contributes to histone deacetylase inhibitor-mediated enhancing effects on apoptosis after ionizing radiation.". Apoptosis 11 (8): 1349–57. doi:10.1007/s10495-006-8266-1. PMID 16830229.
• Schmelzle T, Mailleux AA, Overholtzer M; et al. (2007). "Functional role and oncogene-regulated expression of the BH3-only factor Bmf in mammary epithelial anoikis and morphogenesis.". Proc. Natl. Acad. Sci. U.S.A. 104 (10): 3787–92. doi:10.1073/pnas.0700115104. PMC 1820662. PMID 17360431.
• Yoo NJ, Soung YH, Lee SH; et al. (2007). "Mutational analysis of the BH3 domains of proapoptotic Bcl-2 family genes Bad, Bmf and Bcl-G in laryngeal squamous cell carcinomas.". Tumori 93 (2): 195–7. PMID 17557568.