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J. Biol. Chem., Vol. 275, Issue 29, 22324-22330, July 21, 2000
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From the Departments of Protein kinase C (PKC) regulates fundamental
cellular functions including proliferation, differentiation,
tumorigenesis, and apoptosis. All-trans-retinoic acid
(atRA) modulates PKC activity, but the mechanism of this regulation is
unknown. Amino acid alignments and crystal structure analysis of
retinoic acid (RA)-binding proteins revealed a putative atRA-binding
motif in PKC, suggesting existence of an atRA binding site on the PKC
molecule. This was supported by photolabeling studies showing
concentration- and UV-dependent photoincorporation of
[3H]atRA into PKC
Direct Interaction of All-trans-retinoic Acid with
Protein Kinase C (PKC)
IMPLICATIONS FOR PKC SIGNALING AND CANCER THERAPY*
§,,,,
, and Biochemistry and Molecular
Biology, Pharmacology, ¶ Toxicology, Obstetrics and
Gynecology, and ** Pharmaceutical Sciences, University of Arkansas
for Medical Sciences, Little Rock, Arkansas 72205
, which was effectively protected by
4-OH-atRA, 9-cis-RA, and atRA glucuronide, but not by
retinol. Photoaffinity labeling demonstrated strong competition between
atRA and phosphatidylserine (PS) for binding to PKC, a slight
competition with phorbol-12-myristate-13-acetate, and none with
diacylglycerol, fatty acids, or Ca2+. At pharmacological
concentrations (10 µM), atRA decreased PKC activity
through the competition with PS but not
phorbol-12-myristate-13-acetate, diacylglycerol, or Ca2+.
These results let us hypothesize that in vivo,
pharmacological concentrations of atRA may hamper binding of PS to
PKC and prevent PKC activation. Thus, this study provides the
first evidence for direct binding of atRA to PKC isozymes and suggests
the existence of a general mechanism for regulation of PKC activity
during exposure to retinoids, as in retinoid-based cancer therapy.
*
This work was supported in part by National Institutes of
Health Grants DK51791 and DK49715 (to A. R.-P.) and ES06765 (to V. M. S.) and by an intramural pilot grant (to C. A. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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