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(Received for publication, November 22, 1996)
From the Department of Pharmacology, University of Washington,
Seattle, Washington 98195-7280
Voltage-dependent potentiation of
skeletal muscle L-type calcium channels requires phosphorylation by
cAMP-dependent protein kinase (PKA) that is localized by binding to a
c
Volume 272, Number 10,
Issue of March 7, 1997
pp. 6297-6302
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
MP-dependent protein
inase-
nchoring 
rotein (AKAP).
L-type calcium channels purified from rabbit skeletal muscle contain an
endogenous co-purifying protein kinase activity that phosphorylates the
1 and 
subunits of the channel. The co-purifying kinase also
phosphorylates a known PKA peptide substrate, is stimulated by cAMP,
and is inhibited by PKA inhibitor peptide-(5-24), indicating that it
is PKA. PKA activity co-immunoprecipitates with the calcium channel,
suggesting that the channel and the kinase are physically associated.
Using biotinylated type II regulatory subunit of PKA (RII) as a probe, we have identified a 15-kDa RII-binding protein in purified calcium channel preparations, which we have designated AKAP-15. Anti-peptide antibodies directed against the 1 subunit of the calcium channel co-immunoprecipitate AKAP-15. Together, these findings demonstrate a
physical link between PKA and the calcium channel and suggest that
AKAP-15 may mediate their interaction.
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