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J Biol Chem, Vol. 274, Issue 28, 19852-19861, July 9, 1999
From the Department of Chemistry, University of Illinois,
Chicago, Illinois 60607-7061
The regulatory domain of conventional protein
kinase C (PKC) contains two membrane-targeting modules, the C2 domain
that is responsible for Ca2+-dependent
membrane binding of protein, and the C1 domain composed of two
cysteine-rich zinc fingers (C1a and C1b) that bind diacylglycerols and
phorbol esters. To understand the individual roles and the interplay of
the C1 and C2 domains in the membrane binding and activation of PKC, we
functionally expressed isolated C1 and C2 domains of PKC-
Interplay of C1 and C2 Domains of Protein Kinase C-
in Its
Membrane Binding and Activation
and
measured their vesicle binding and monolayer penetration. Results
indicate that the C2 domain of PKC- is responsible for the initial
Ca2+- and phosphatidylserine-dependent
electrostatic membrane binding of PKC-, whereas the C1 domain is
involved in subsequent membrane penetration and diacylglycerol binding,
which eventually lead to enzyme activation. To determine the roles of
individual zinc fingers in the C1 domain, we also mutated hydrophobic
residues in the C1a (Trp58 and Phe60) and C1b
(Tyr123 and Leu125) domains of the native
PKC- molecule and measured the effects of mutations on vesicle
binding, enzyme activity and monolayer penetration. Results show that
the hydrophobic residues in the C1a domain are essential for the
membrane penetration and activation of PKC-, whereas those in the
C1b domain are not directly involved in these processes. Based on these
results in conjunction with our previous structure-function studies of
the C2 domain (Medkova, M., and Cho, W. (1998) J. Biol.
Chem. 273, 17544-17552), we propose a mechanism for the in
vitro membrane binding and activation of conventional PKC that
accounts for the temporal and spatial sequences of PKC activation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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