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First published online March 5, 2008

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PKC-Abl: stressed to death

The unfolded protein response (UPR) is an ER-stress-induced signalling cascade that is activated by the accumulation of misfolded proteins within the ER, and either restores proper protein folding or leads to apoptotic cell death. The mechanism responsible for ER-stress-induced cell death is unclear, but on page 804, Xin Qi and Daria Mochly-Rosen describe a possible role for PKC and the receptor tyrosine kinase Abl in culture as well as in an in vivo stroke model. Using a variety of biochemical and imaging studies, the authors implicate the ER-stress-induced apoptosis pathway in Neuro2a cells treated with tunicamycin and also in focal cerebral ischemia in the rat. They report that ER stress induces translocation of PKC from the cytosol to the ER, where it binds to Abl. This complex then moves to the mitochondria, where it activates JNK signalling and contributes to ER-stress-induced apoptosis. These results represent a potential mechanism by which cells modulate apoptosis in response to ER stress.

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Related articles in JCS:

The PKC -Abl complex communicates ER stress to the mitochondria – an essential step in subsequent apoptosis

Xin Qi and Daria Mochly-Rosen
JCS 2008 121: 804-813. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?