Bcl-2-associated death promoter: Difference between revisions
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{{PBB|geneid=572}} |
{{PBB|geneid=572}} |
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The '''Bcl-2-associated death promoter''' (BAD) [[protein]] is a [[apoptosis|pro-apoptotic]] member of the [[Bcl-2]] gene family which is involved in initiating [[apoptosis]]. It does not contain a [[C-terminal]] transmembrane [[protein domain|domain]] for outer [[mitochondrial membrane]] and [[nuclear envelope]] targeting, unlike most other members of the Bcl-2 family |
The '''Bcl-2-associated death promoter''' ('''BAD''') [[protein]] is a [[apoptosis|pro-apoptotic]] member of the [[Bcl-2]] gene family which is involved in initiating [[apoptosis]]. It does not contain a [[C-terminal]] transmembrane [[protein domain|domain]] for outer [[mitochondrial membrane]] and [[nuclear envelope]] targeting, unlike most other members of the Bcl-2 family |
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<ref name="sheau">{{cite journal | author=Sheau Yu Hsu, ''et al.''| title=Interference of BAD (Bcl-xL/Bcl-2-Associated Death Promoter)-Induced Apoptosis in Mammalian Cells by 14–3-3 Isoforms and P11| journal=Molecular Endocrinology| year=1997| volume=11| issue=12| url=http://mend.endojournals.org/cgi/content/full/11/12/1858| pages=1858–1867| doi=10.1210/me.11.12.1858}}</ref>. |
<ref name="sheau">{{cite journal | author=Sheau Yu Hsu, ''et al.''| title=Interference of BAD (Bcl-xL/Bcl-2-Associated Death Promoter)-Induced Apoptosis in Mammalian Cells by 14–3-3 Isoforms and P11| journal=Molecular Endocrinology| year=1997| volume=11| issue=12| url=http://mend.endojournals.org/cgi/content/full/11/12/1858| pages=1858–1867| doi=10.1210/me.11.12.1858}}</ref>. |
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Pro-apoptotic activation of this protein occurs through [[phosphorylation]]<ref name="entrez">{{Cite web|url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=572|title=Entrez Gene entry for BAD|accessdate=2006-12-19|publisher=NCBI}}</ref>. After activation, it is able to form a [[heterodimer]] with anti-apoptotic proteins and prevent them from stopping apoptosis. |
Pro-apoptotic activation of this protein occurs through [[phosphorylation]]<ref name="entrez">{{Cite web|url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=572|title=Entrez Gene entry for BAD|accessdate=2006-12-19|publisher=NCBI}}</ref>. After activation, it is able to form a [[heterodimer]] with anti-apoptotic proteins and prevent them from stopping apoptosis. |
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Revision as of 18:23, 17 October 2008
Template:PBB The Bcl-2-associated death promoter (BAD) protein is a pro-apoptotic member of the Bcl-2 gene family which is involved in initiating apoptosis. It does not contain a C-terminal transmembrane domain for outer mitochondrial membrane and nuclear envelope targeting, unlike most other members of the Bcl-2 family [1]. Pro-apoptotic activation of this protein occurs through phosphorylation[2]. After activation, it is able to form a heterodimer with anti-apoptotic proteins and prevent them from stopping apoptosis.
BAD is a member of the BH3-only family [3], a subfamily of the Bcl-2 family.
The Bcl-2-associated death promoter (BAD) protein is a member of the Bcl-2 gene family. Some members of this family are pro-apoptotic (e.g., Bax, Bak) while others are anti-apoptotic (e.g., Bcl-2, Bcl-xL). Bax/Bak are believed to initiate apoptosis by forming a pore in the mitochondrial outer membrane that allows cytochrome c to escape into the cytoplasm and activate the pro-apoptotic caspase cascade. The anti-apoptotic Bcl proteins inhibit cytochrome c release through the mitochondrial pore and also inhibit activation of the cytoplasmic caspase cascade by cytochrome c.[4]
BAD does not contain a C-terminal transmembrane domain for outer mitochondrial membrane and nuclear envelope targeting, unlike most other members of the Bcl-2 family [1]. BAD is a member of the BH3-only family [3], a subfamily of the Bcl-2 family.
Dephosphorylated BAD forms a heterodimer with Bcl-2 and Bcl-xL, inactivating them and thus allowing Bax/Bak-triggered apoptosis. On the other hand, BAD phosphorylation by Akt/protein kinase B (triggered by PIP3), causes formation of the BAD-(14-3-3)protein heterodimer. This leaves Bcl-2 free to inhibit Bax-triggered apoptosis.[5] BAD phosphorylation is thus anti-apoptotic, and BAD dephosphorylation (e.g., by Ca++-stimulated Calcineurin) is pro-apoptotic. The latter may be involved in neural diseases such as schizophrenia.[6]
See also
References
- ^ Sheau Yu Hsu; et al. (1997). "Interference of BAD (Bcl-xL/Bcl-2-Associated Death Promoter)-Induced Apoptosis in Mammalian Cells by 14–3-3 Isoforms and P11". Molecular Endocrinology. 11 (12): 1858–1867. doi:10.1210/me.11.12.1858.
{{cite journal}}: Explicit use of et al. in:|author=(help) - ^ "Entrez Gene entry for BAD". NCBI. Retrieved 2006-12-19.
- ^ Adachi M. and Imai K. (2002). "The proapoptotic BH3-only protein BAD transduces cell death signals independently of its interaction with Bcl-2". Cell death and differentiation. 9 (11): 1240–1247. doi:10.1038/sj.cdd.4401097.
- ^ Helmreich, E.J.M. (2001) The Biochemistry of Cell Signalling, pp. 238-43
- ^ E.J.M. (2001) The Biochemistry of Cell Signalling, pp. 242
- ^ Foster, T.C. et al (2001) J. Neurosci. 21, 4066-4073, "Calcineurin Links Ca++ Dysregulation with Brain Aging"(
Further reading
External links
- bcl-Associated+Death+Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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