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(Received for publication, January 11, 1996, and in revised form, March 27, 1996)
From the Cardiovascular Research Institute and Daiichi Research
Center, University of California at San Francisco,
San Francisco, California 94143
We report the identification of a novel class of
phosphatidylinositol (PtdIns) 3-kinases whose members
contain C-terminal C2 domains. We have isolated
Drosophila and murine genes (termed cpk and
cpk-m respectively) by polymerase chain
reaction amplification of cDNA libraries with degenerate primers
corresponding to conserved regions of PtdIns kinases. The amino acid
sequences of Cpk and Cpk-m are most similar to that of p110, a family
of PtdIns 3-kinases that mediates the responses of cells to mitogenic
stimuli. The Cpk and Cpk-m sequences are similar to a large, central
region of p110, but differ from p110 at their N and C termini. The N
termini of the Cpk proteins do not contain any recognizable protein
motif, while the C termini contain ``C2 domains,'' a feature unique
among PtdIns kinases. Cpk has an intrinsic PtdIns kinase activity and
can phosphorylate PtdIns and PtdIns-4-P, but not
PtdIns(4,5)P2, at the D3 position of the inositol ring. Cpk
is the first PtdIns 3-kinase identified with this particular
substrate specificity. We have identified two potential Cpk-binding
proteins, p90 and p190, and have determined that both Cpk and p190 may
be tyrosine phosphorylated. This finding suggests that Cpk function may
be regulated by tyrosine kinases.
Volume 271, Number 23,
Issue of June 7, 1996
pp. 13892-13899
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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