Abstract
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
Current Molecular Medicine
Title: Regulation of Bcl-2 Family Proteins by Posttranslational Modifications
Volume: 8 Issue: 2
Author(s): Anthony Letai and Ozgur Kutuk
Affiliation:
Keywords: proteosome, kinase, phosphorylation, BAD, BID, BIM, BAX, BH3-only, apoptosis, BCL-2
Abstract: 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.
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Cite this article as:
Letai Anthony and Kutuk Ozgur, Regulation of Bcl-2 Family Proteins by Posttranslational Modifications, Current Molecular Medicine 2008; 8 (2) . https://dx.doi.org/10.2174/156652408783769599
DOI https://dx.doi.org/10.2174/156652408783769599 |
Print ISSN 1566-5240 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5666 |
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