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J Biol Chem, Vol. 274, Issue 14, 9224-9230, April 2, 1999
Isoform of Protein Kinase C
From the Department of Medicine, School of Medicine and Molecular
Biology Institute, University of California, Los Angeles, California
90095-1786 and the Imperial Cancer Research Fund, 44 Lincoln's Inn
Fields, London, WC2A 3PX, United Kingdom
The results presented here demonstrate that
protein kinase D (PKD) and PKC
transiently coexpressed in COS-7
cells form complexes that can be immunoprecipitated from cell lysates
using specific antisera to PKD or PKC. The presence of PKC in PKD
immune complexes was initially detected by in vitro kinase
assays which reveal the presence of an 80-kDa phosphorylated band in
addition to the 110-kDa band corresponding to autophosphorylated PKD.
The association between PKD and PKC was further verified by Western
blot analysis and peptide phosphorylation assays that exploited the
distinct substrate specificity between PKCs and PKD. By the same
criteria, PKD formed complexes only very weakly with PKC
, and did
not bind PKC
. When PKC was coexpressed with PKD mutants
containing either complete or partial deletions of the PH domain, both
PKC immunoreactivity and PKC activity in PKD immunoprecipitates were
sharply reduced. In contrast, deletion of an amino-terminal portion of
the molecule, either cysteine-rich region, or the entire cysteine-rich
domain did not interfere with the association of PKD with PKC.
Furthermore, a glutathione S-transferase-PKDPH fusion
protein bound preferentially to PKC. These results indicate that the
PKD PH domain can discriminate between closely related structures of a
single enzyme family, e.g. novel PKCs and , thereby
revealing a previously undetected degree of specificity among
protein-protein interactions mediated by PH domains.
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