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J Biol Chem, Vol. 274, Issue 16, 10765-10770, April 16, 1999
PKC but Not 
/
PKC by Caspase-3 during
UV-induced Apoptosis
From the Laboratorio Glaxo Wellcome-CSIC de Biología
Molecular y Celular, Centro de Biología Molecular "Severo
Ochoa" (Consejo Superior de Investigaciones
Científicas-Universidad Autónoma de Madrid), Universidad
Autónoma, Canto Blanco, 28049 Madrid, Spain
The stimulation of caspases is a critical event
in apoptotic cell death. Several kinases critically involved in
cell proliferation pathways have been shown to be cleaved by
caspase-mediated mechanisms. Thus, the degradation of 
protein
kinase C (PKC) and MEKK-1 by caspase-3 generates activated fragments
corresponding to their catalytic domains, consistent with the
observations that both enzymes are important for apoptosis. In
contrast, other kinases reported to have anti-apoptotic properties,
such as Raf-1 and Akt, are inactivated by proteolytic degradation by
the caspase system. Since the atypical PKCs have been shown to play
critical roles in cell survival, in the study reported here we have
addressed the potential degradation of these PKCs by the caspase system in UV-irradiated HeLa cells. Herein we show that although 
PKC and
/
PKC are both inhibited in UV-treated cells, only PKC but not
/PKC is cleaved by a caspase-mediated process. This cleavage generates a fragment that corresponds to its catalytic domain that is
enzymatically inactive. The sequence where caspase-3 cleaves PKC was
mapped, and a mutant resistant to degradation was shown to protect
cells from apoptosis more efficiently than the wild-type enzyme.
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