Zinc induces specific association of PKC with membrane cytoskeleton.
Putative binding sites for zinc are present in the regulatory domain of protein kinase C but a distinct role for zinc has not yet been proposed. Here we show that micromolar concentrations of zinc chloride cause pure rat brain protein kinase C to localize in a detergent-insoluble, cytoskeletal fraction of red cell membranes and to bind to isolated cytoskeleton in the presence of phosphatidylserine. Attachment of protein kinase C to cytoskeleton was accompanied by enhanced expression of binding sites for 3H-phorbol ester, a regulatory ligand of protein kinase C. The active factor in the cytoskeleton was labile to protease suggesting that protein kinase C binds to a cytoskeletal protein.
Forbes
I J
IJ
Department of Medicine, University of Adelaide, Woodville, South Australia.
Zalewski
P D
PD
Giannakis
C
C
Betts
W H
WH
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000201:enzymology; D002118:Calcium / Q000378:metabolism; D003599:Cytoskeleton / Q000201:enzymology* / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000201:enzymology* / Q000378:metabolism; D010703:Phorbol Esters / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D012995:Solubility; D015032:Zinc / Q000494:pharmacology*
D010703:Phorbol Esters; D010718:Phosphatidylserines; D011493:Protein Kinase C; D015032:Zinc; D002118:Calcium