Journal
ONCOGENE
Volume 27, Issue -, Pages S137-S148Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2009.51
Keywords
Beclin 1; autophagy; BH3-only; apoptosis; Bcl-2; tumor suppressor
Funding
- NIH [R21 AI78108-01, RO1 CA109618, R01 CA084254]
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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. Oncogene (2009) 27, S137-S148; doi: 10.1038/onc.2009.51
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