[Phosphorylation of cytoplasmic poly (ADP-ribose) polymerase linked to free ribonucleoprotein particles by an associated protein kinase C].
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.
Chypre
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C
Centre de Neurochimie, Strasbourg.
Le Calvez
C
C
Hog
F
F
Revel
M O
MO
Jesser
M
M
Mandel
P
P
D015153:Blotting, Western; D003593:Cytoplasm / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D010766:Phosphorylation; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism*
D012333:RNA, Messenger; D012261:Ribonucleoproteins; D011065:Poly(ADP-ribose) Polymerases; D011493:Protein Kinase C
Phosphorylation de la poly (ADP-ribose) polymérase cytoplasmique liée à des particules ribonucléoprotéiques libres par une protéine kinase C associée.