Tyrosine 311 is phosphorylated by c-Abl and promotes the apoptotic effect of PKCdelta in glioma cells

In this study we characterized the phosphorylation of tyrosine 311 and its role in the apoptotic function of PKCdelta in glioma cells. We found that c-Abl phosphorylated PKCdelta on tyrosine 311 in response to H2O2 and that this phosphorylation contributed to the apoptotic effect of H2O2. In contras...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-01, Vol.352 (2), p.431-436
Main Authors: Lu, Wei, Finnis, Susan, Xiang, Cunli, Lee, Hae Kyung, Markowitz, Yael, Okhrimenko, Hana, Brodie, Chaya
Format: Article
Language:English
Subjects:
Apoptosis
Binding Sites
Cell Line, Tumor
Glioma - metabolism
Glioma - pathology
Humans
Phosphorylation
Protein Binding
Protein Kinase C-delta - metabolism
Proto-Oncogene Proteins c-abl - metabolism
Tyrosine - metabolism
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Summary:In this study we characterized the phosphorylation of tyrosine 311 and its role in the apoptotic function of PKCdelta in glioma cells. We found that c-Abl phosphorylated PKCdelta on tyrosine 311 in response to H2O2 and that this phosphorylation contributed to the apoptotic effect of H2O2. In contrast, Src, Lyn, and Yes were not involved in the phosphorylation of tyrosine 311 by H2O2. A phosphomimetic PKCdelta mutant, in which tyrosine 311 was mutated to glutamic acid (PKCdeltaY311E), induced a large degree of cell apoptosis. Overexpression of the PKCdeltaY311E mutant induced the phosphorylation of p38 and inhibition of p38 abolished the apoptotic effect of the PKCdelta mutant. These results suggest an important role of tyrosine 311 in the apoptotic function of PKCdelta and implicate c-Abl as the kinase that phosphorylates this tyrosine.
ISSN:0006-291X