[Phosphorylation of cytoplasmic poly (ADP-ribose) polymerase linked to free ribonucleoprotein particles by an associated protein kinase C] - PubMed (original) (raw)
[Article in French]
Affiliations
- PMID: 2516473
[Phosphorylation of cytoplasmic poly (ADP-ribose) polymerase linked to free ribonucleoprotein particles by an associated protein kinase C]
[Article in French]
C Chypre et al. C R Acad Sci III. 1989.
Abstract
Considering the eventuality of an interaction between the two post-translational modifications, phosphorylation and ADP-ribosylation, we investigated the possibility of phosphorylation of the mRNP polyADPR polymerase by a protein kinase C associated to these particles. We demonstrated that cytoplasmic poly (ADP-ribose) polymerase associated with ribonucleoprotein particles containing silent mRNA is phosphorylated by a specifically activated endogenous protein kinase C which in turn induces an inhibition of the polymerase activity. In the absence of protein kinase C activators the mRNP polyADPR-P is also phosphorylated but without changes of its enzymatic activity.
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