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Volume 272, Number 7, Issue of February 14, 1997 pp. 4072-4078
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Conventional PKC-alpha , Novel PKC-epsilon and PKC-theta , but Not Atypical PKC-lambda Are MARCKS Kinases in Intact NIH 3T3 Fibroblasts

(Received for publication, July 10, 1996, and in revised form, October 11, 1996)

Florian Überall Dagger , Sabine Giselbrecht Dagger , Karina Hellbert Dagger , Friedrich Fresser , Birgit Bauer , Michael Gschwendt par , Hans H. Grunicke Dagger and Gottfried Baier

From the Dagger  Institute of Medical Chemistry and Biochemistry, University of Innsbruck, the par  German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Federal Republic of Germany, and the  Institute of Medical Biology and Human Genetics, University of Innsbruck, A-6020 Innsbruck, Austria

Phosphorylation of myristoylated alanine-rich protein kinase C substrate (MARCKS) in intact cells has been employed as an indicator for activation of protein kinase C (PKC). Specific PKC isoenzymes responsible for MARCKS phosphorylation under physiological conditions, however, remained to be identified. In our present study using stably transfected NIH 3T3 cell clones we demonstrate that expression of constitutively active mutants of either conventional cPKC-alpha or novel nPKC-epsilon increased phosphorylation of endogenous MARCKS in the absence of phorbol 12,13-dibutyrate in intact mouse fibroblasts, implicating that each of these PKC isoforms itself is sufficient to induce enhanced MARCKS phosphorylation. Similarly, ectopic expression of a constitutively active mutant of PKC-theta significantly increased MARCKS phosphorylation compared to vector controls, identifying PKC-theta as a MARCKS kinase. The PKC-specific inhibitor GF 109203X (bisindolylmaleimide I) reduced MARCKS phosphorylation in intact cells at a similar dose-response as enzymatic activity of recombinant isoenzymes cPKC-alpha , nPKC-epsilon , and nPKC-theta in vitro. Consistently, phorbol 12,13-dibutyrate-dependent MARCKS phosphorylation was significantly reduced in cell lines expressing dominant negative mutants of either PKC-alpha K368R or (dominant negative) PKC-epsilon K436R. The fact, that the constitutively active PKC-lambda A119E mutant did not alter the MARCKS phosphorylation underscores the assumption that atypical PKC isoforms are not involved in this process. We conclude that under physiological conditions, conventional cPKC-alpha and novel nPKC-epsilon , but not atypical aPKC-lambda are responsible for MARCKS phosphorylation in intact NIH 3T3 fibroblasts.


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