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Title: Bcl-2 phosphorylation and implications in apoptosis in cancer cells
Authors: Xia, Yan
Keywords: DRNTU::Science::Biological sciences::Molecular biology
Issue Date: 2011
Abstract: Bcl-2 is the central regulator in apoptosis. Structural studies of Bcl-2 reveal a flexible loop flanking the Bcl-2 homology domain 3 (BH3) and BH4. In response to external stimuli, several kinases phosphorylate the loop of Bcl-2. Phosphorylation on Bcl-2 has been thought to affect the protein’s activity in apoptosis as well as autophagy. However, the molecular basis and mechanistic details of Bcl-2 phosphorylation still remains a mystery. To further define and better understand the biological significance and the regulation of Bcl-2 through phosphorylation, we focus on changes in molecular interaction, using a phospho-mimetic Bcl-2 as a model. Our structural analysis indicates phosphorylation would induce conformational change in the flexible loop of Bcl-2. Binding study revealed phospho-mimetic Bcl-2 has decreased affinity to pro-apoptotic protein Bak. Based on our result, we hypothesized the structural-function relationship for Bcl-2 phosphorylation.
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)

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