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J Biol Chem, Vol. 273, Issue 36, 23126-23133, September 4, 1998
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From the Protein kinase Cµ (PKCµ), also named protein
kinase D, is an unusual member of the PKC family that has a putative
transmembrane domain and pleckstrin homology domain. This enzyme has a
substrate specificity distinct from other PKC isoforms (Nishikawa, K.,
Toker, A., Johannes, F. J., Songyang, Z., and Cantley, L. C. (1997) J. Biol. Chem. 272, 952-960), and its
mechanism of regulation is not yet clear. Here we show that PKCµ
forms a complex in vivo with a phosphatidylinositol
4-kinase and a phosphatidylinositol-4-phosphate 5-kinase. A region of
PKCµ between the amino-terminal transmembrane domain and the
pleckstrin homology domain is shown to be involved in the association
with the lipid kinases. Interestingly, a kinase-dead point mutant of
PKCµ failed to associate with either lipid kinase activity,
indicating that autophosphorylation may be required to expose the lipid
kinase interaction domain. Furthermore, the subcellular distribution of
the PKCµ-associated lipid kinases to the particulate fraction depends
on the presence of the amino-terminal region of PKCµ including the
predicted transmembrane region. These results suggest a novel model in
which the non-catalytic region of PKCµ acts as a scaffold for
assembly of enzymes involved in phosphoinositide synthesis at specific
membrane locations.
Division of Signal Transduction, Beth Israel
Deaconess Medical Center and Department of Cell Biology, Harvard
Medical School, Boston, Massachusetts 02115, the ¶ Boston
Biomedical Research Institute, Boston, Massachusetts 02114, and the
Institute of Cell Biology and Immunology, University of
Stuttgart, Allmandring 31, 70569 Stuttgart, Germany
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