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Oncogene. 2008 Dec;27 Suppl 1:S137-48. doi: 10.1038/onc.2009.51.

The autophagy effector Beclin 1: a novel BH3-only protein.

Author information

1
Department of Chemistry, Biochemistry and Molecular Biology, North Dakota State University, Fargo, ND, USA. Sangita.Sinha@ndsu.edu

Abstract

BH3 domains were originally discovered in the context of apoptosis regulators and they mediate binding of proapoptotic Bcl-2 family members to antiapoptotic Bcl-2 family members. Yet, recent studies indicate that BH3 domains do not function uniquely in apoptosis regulation; they also function in the regulation of another critical pathway involved in cellular and tissue homeostasis called autophagy. Antiapoptotic Bcl-2 homologs downregulate autophagy through interactions with the essential autophagy effector and haploinsufficient tumor suppressor, Beclin 1. Beclin 1 contains a BH3 domain, similar to that of Bcl-2 proteins, which is necessary and sufficient for binding to antiapoptotic Bcl-2 homologs and required for Bcl-2-mediated inhibition of autophagy. This review will summarize the evidence that the BH3 domain of Beclin 1 serves as a key structural motif that enables Bcl-2 to function not only as an antiapoptotic protein, but also as an antiautophagy protein.

PMID:
19641499
PMCID:
PMC2731580
DOI:
10.1038/onc.2009.51
[Indexed for MEDLINE]
Free PMC Article

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