- BMF (gene)
Bcl2 modifying factor, also known as BMF, is a human
gene .cite web | title = Entrez Gene: BMF Bcl2 modifying factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=90427| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: BMF Bcl2 modifying factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=90427| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Hattori A, Okumura K, Nagase T, "et al." |title=Characterization of long cDNA clones from human adult spleen. |journal=DNA Res. |volume=7 |issue= 6 |pages= 357–66 |year= 2001 |pmid= 11214971 |doi=
*cite journal | author=Puthalakath H, Villunger A, O'Reilly LA, "et al." |title=Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. |journal=Science |volume=293 |issue= 5536 |pages= 1829–32 |year= 2001 |pmid= 11546872 |doi= 10.1126/science.1062257
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Lei K, Davis RJ |title=JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 5 |pages= 2432–7 |year= 2003 |pmid= 12591950 |doi= 10.1073/pnas.0438011100
*cite journal | author=Day CL, Puthalakath H, Skea G, "et al." |title=Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. |journal=Biochem. J. |volume=377 |issue= Pt 3 |pages= 597–605 |year= 2004 |pmid= 14561217 |doi= 10.1042/BJ20031251
*cite journal | author=Morales AA, Olsson A, Celsing F, "et al." |title=Expression and transcriptional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells. |journal=Leukemia |volume=18 |issue= 1 |pages= 41–7 |year= 2004 |pmid= 14574334 |doi= 10.1038/sj.leu.2403183
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Chen L, Willis SN, Wei A, "et al." |title=Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. |journal=Mol. Cell |volume=17 |issue= 3 |pages= 393–403 |year= 2005 |pmid= 15694340 |doi= 10.1016/j.molcel.2004.12.030
*cite journal | author=Kuwana T, Bouchier-Hayes L, Chipuk JE, "et al." |title=BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. |journal=Mol. Cell |volume=17 |issue= 4 |pages= 525–35 |year= 2005 |pmid= 15721256 |doi= 10.1016/j.molcel.2005.02.003
*cite journal | author=Soung YH, Lee JW, Park WS, "et al." |title=BH3 domain mutation of proapoptotic genes Bad, Bmf and Bcl-G is rare in transitional cell carcinomas of the urinary bladder. |journal=Pathology |volume=38 |issue= 1 |pages= 33–4 |year= 2006 |pmid= 16484005 |doi= 10.1080/00313020500455811
*cite journal | author=Zhang Y, Adachi M, Kawamura R, "et al." |title=Bmf contributes to histone deacetylase inhibitor-mediated enhancing effects on apoptosis after ionizing radiation. |journal=Apoptosis |volume=11 |issue= 8 |pages= 1349–57 |year= 2007 |pmid= 16830229 |doi= 10.1007/s10495-006-8266-1
*cite journal | author=Schmelzle T, Mailleux AA, Overholtzer M, "et al." |title=Functional role and oncogene-regulated expression of the BH3-only factor Bmf in mammary epithelial anoikis and morphogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 10 |pages= 3787–92 |year= 2007 |pmid= 17360431 |doi= 10.1073/pnas.0700115104
*cite journal | author=Yoo NJ, Soung YH, Lee SH, "et al." |title=Mutational analysis of the BH3 domains of proapoptotic Bcl-2 family genes Bad, Bmf and Bcl-G in laryngeal squamous cell carcinomas. |journal=Tumori |volume=93 |issue= 2 |pages= 195–7 |year= 2007 |pmid= 17557568 |doi=PBB_Controls
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