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Current Molecular Medicine


ISSN (Print): 1566-5240
ISSN (Online): 1875-5666

Regulation of Bcl-2 Family Proteins by Posttranslational Modifications

Author(s): Anthony Letai and Ozgur Kutuk

Volume 8, Issue 2, 2008

Page: [102 - 118] Pages: 17

DOI: 10.2174/156652408783769599

Price: $65


Like many proteins, function and abundance of Bcl-2 family proteins are influenced by posttranslational modifications. These modifications include phosphorylation, proteolytic cleavage, ubiquitination, and proteosomal degradation. These modifications, depending on cellular context and the proteins involved, can result either in a promotion of inhibition of apoptosis. Many of these modifications are governed by the activity of enzymes. As modulation of enzymatic activity can be achieved fairly efficiently using small molecules, understanding the effects of posttranslational modifications may allow for the therapeutic inhibition or promotion of apoptosis.

Keywords: proteosome, kinase, phosphorylation, BAD, BID, BIM, BAX, BH3-only, apoptosis, BCL-2

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