Regulation of protein kinase C by Zn(2+)-dependent interaction with actin.
Zn2+ influences diverse cellular processes by poorly understood mechanisms. Some of these effects may be mediated by the protein kinase C (PKC) family of enzymes, since an influx of Zn2+ greatly increases their binding of regulatory ligand phorbol ester and induces their translocation from cytosol to the cytoskeleton. Using a model with purified components, we now show that Zn2+ acts by forming a phospholipid-dependent complex of PKC with filamentous actin, which results in expression of new binding sites for phorbol ester and phosphorylation of actin. These results provide a basis for the observed localization of PKC at actin-membrane junctions, in-vivo.
Zalewski
P D
PD
Department of Medicine, University of Adelaide, Woodville, South Australia.
Forbes
I J
IJ
Giannakis
C
C
Betts
W H
WH
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002712:Chlorides / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D015240:Phorbol 12,13-Dibutyrate / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D015032:Zinc / Q000494:pharmacology*; D017967:Zinc Compounds
D000199:Actins; D002712:Chlorides; D017967:Zinc Compounds; D015240:Phorbol 12,13-Dibutyrate; C016837:zinc chloride; D011493:Protein Kinase C; D015032:Zinc