Vol 42: Protein kinase C controls activation of the DNA integrity checkpoint.Report as inadecuate



 Vol 42: Protein kinase C controls activation of the DNA integrity checkpoint.


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This article is from Nucleic Acids Research, volume 42.AbstractThe protein kinase C PKC superfamily plays key regulatory roles in numerous cellular processes. Saccharomyces cerevisiae contains a single PKC, Pkc1, whose main function is cell wall integrity maintenance. In this work, we connect the Pkc1 protein to the maintenance of genome integrity in response to genotoxic stresses. Pkc1 and its kinase activity are necessary for the phosphorylation of checkpoint kinase Rad53, histone H2A and Xrs2 protein after deoxyribonucleic acid DNA damage, indicating that Pkc1 is required for activation of checkpoint kinases Mec1 and Tel1. Furthermore, Pkc1 electrophoretic mobility is delayed after inducing DNA damage, which reflects that Pkc1 is post-translationally modified. This modification is a phosphorylation event mediated by Tel1. The expression of different mammalian PKC isoforms at the endogenous level in yeast pkc1 mutant cells revealed that PKCĪ“ is able to activate the DNA integrity checkpoint. Finally, downregulation of PKCĪ“ activity in HeLa cells caused a defective activation of checkpoint kinase Chk2 when DNA damage was induced. Our results indicate that the control of the DNA integrity checkpoint by PKC is a mechanism conserved from yeast to humans.



Author: Soriano-Carot, Maria; Quilis, Inma; Bano, M. Carmen; Igual, J. Carlos

Source: https://archive.org/







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