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Phosphorylation of the Conditioning‐Associated GTP‐Binding Protein cp20 by Protein Kinase C
Author(s) -
Nelson T. J.,
Alkon D. L.
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.65052350.x
Subject(s) - phosphorylation , protein kinase c , biology , protein kinase a , microbiology and biotechnology , gtp' , biochemistry , map2k7 , kinase , cytosol , cyclin dependent kinase 2 , enzyme
The phosphorylation state of cp20, a low molecular weight membrane‐associated GTP‐binding protein, was previously shown to increase two‐ to threefold 24 h after associative conditioning. Here, cp20 is shown to be phosphorylated by protein kinase C (PKC) in vitro. Pronounced differences in activity were observed with the three major isoforms of PKC, whereas casein kinase, calcium/calmodulin‐dependent protein kinase II, and cyclic AMP‐dependent protein kinase produced no detectable phosphorylation of cp20. Phosphorylation of cp20 had no effect on its GTPase or GTP‐binding activity but caused a translocation of cp20 from cytosol to the nuclei/mitochondrial particulate fraction. These results suggest that the increase in phosphorylation of cp20 after conditioning may be due to PKC.