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Vol. 8, Issue 10, 1889-1899, October 1997
and
*Department of Biochemistry, Hadassah Medical School, The Hebrew
University, Jerusalem 91120, Israel; and
Myosin II heavy chain (MHC) specific protein kinase C (MHC-PKC),
isolated from Dictyostelium discoideum, regulates myosin II assembly and localization in response to the chemoattractant cyclic
AMP. Immunoprecipitation of MHC-PKC revealed that it resides as a
complex with several proteins. We show herein that one of these
proteins is a homologue of the 14-3-3 protein (Dd14-3-3). This
protein has recently been implicated in the regulation of intracellular
signaling pathways via its interaction with several signaling proteins,
such as PKC and Raf-1 kinase. We demonstrate that the mammalian 14-3-3
Laboratory of
Protein Structure, National Institute for Medical Research, London NW7
1AA, United Kingdom
isoform inhibits the MHC-PKC activity in vitro and that this
inhibition is carried out by a direct interaction between the two
proteins. Furthermore, we found that the cytosolic MHC-PKC, which is
inactive, formed a complex with Dd14-3-3 in the cytosol in a cyclic
AMP-dependent manner, whereas the membrane-bound active MHC-PKC was not
found in a complex with Dd14-3-3. This suggests that Dd14-3-3
inhibits the MHC-PKC in vivo. We further show that MHC-PKC binds
Dd14-3-3 as well as 14-3-3 through its C1 domain, and the
interaction between these two proteins does not involve a peptide
containing phosphoserine as was found for Raf-1 kinase. Our experiments
thus show an in vivo function for a member of the 14-3-3 family and
demonstrate that MHC-PKC interacts directly with Dd14-3-3 and
14-3-3 through its C1 domain both in vitro and in vivo, resulting
in the inhibition of the kinase.
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