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J. Biol. Chem., Vol. 277, Issue 25, 22925-22933, June 21, 2002
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From the Protein kinase C (PKC) regulation of
cystic fibrosis transmembrane regulator (CFTR) chloride function
has been demonstrated in several cell lines, including Calu-3 cells
that express native, wild-type CFTR. We demonstrated previously that
PKC
Protein Kinase C
-dependent Regulation of Cystic
Fibrosis Transmembrane Regulator Involves Binding to a Receptor for
Activated C Kinase (RACK1) and RACK1 Binding to
Na+/H+ Exchange Regulatory Factor*
§,, and
Warren Alan Bernbaum, M.D. Center for Cystic
Fibrosis Research, Departments of Pediatrics at Rainbow Babies and
Children Hospital, and Physiology and Biophysics, Case Western Reserve
University, Cleveland, Ohio 44106-4948 and the ¶ Department of
Gastroenterology, Division of Digestive Diseases, Department of
Medicine, Emory University, Atlanta, Georgia 30322
was required for cAMP-dependent CFTR function. The
goal of this study was to determine whether PKC interacts directly
with CFTR. Using overlay assay, immunoprecipitation, pulldown and
binding assays, we show that PKC does not bind to CFTR, but does
bind to a receptor for activated C kinase (RACK1), a 37-kDa scaffold
protein, and that RACK1 binds to Na+/H+
exchange regulatory factor (NHERF1), a binding partner of CFTR. In vitro binding assays demonstrate
dose-dependent binding of PKC to RACK1 which is
inhibited by an 8-amino acid peptide based on the sequence of the sixth
Trp-Asp repeat in RACK1 or by an 8-amino acid sequence in the V1 region
of PKC, V1-2. A 4-amino acid sequence INAL (70-73) expressed in
CFTR shares 50% homology to the RACK1 inhibitory peptide, but it does
not bind PKC. NHERF1 and RACK1 bind in a dose-dependent
manner. Immunofluorescence and confocal microscopy of RACK1 and CFTR
revealed colocalization of the proteins to the apical and lateral
regions of Calu-3 cells. The results indicate the RACK1 binds PKC
and NHERF1, thus serving as a scaffold protein to anchor the enzyme in
proximity to CFTR.
*
This work was supported by National Institutes of Health
Grants HL58598, HL67190, and DK44484, Cystic Fibrosis Core Center Grant
DK27651, Cystic Fibrosis Foundation Grant LIEDTK00G0, and a research
development program.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 © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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