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J Biol Chem, Vol. 273, Issue 30, 18930-18935, July 24, 1998
From the Intracellular Ca2+
release in muscle is governed by functional communication between the
voltage-dependent L-type Ca2+ channel and the
intracellular Ca2+ release channel by processes that are
incompletely understood. We previously showed that sorcin binds to
cardiac Ca2+ release channel/ryanodine receptors and
decreases channel open probability in planar lipid bilayers. In
addition, we showed that sorcin antibody immunoprecipitates ryanodine
receptors from metabolically labeled cardiac myocytes along with a
second protein having a molecular weight similar to that of the
Sorcin Associates with the Pore-forming Subunit of
Voltage-dependent L-type Ca2+ Channels
,,
Department of Medicine, Cardiovascular
Institute, Mount Sinai School of Medicine, New York, New York 10029 and
the ¶ Department of Molecular Pharmacology and Biological
Chemistry, Northwestern University Medical School,
Chicago, Illinois 60611
1 subunit of cardiac L-type Ca2+ channels.
We now demonstrate that sorcin biochemically associates with cardiac
and skeletal muscle L-type Ca2+ channels specifically
within the cytoplasmically oriented C-terminal region of the
1 subunits, providing evidence that the second protein
recovered by sorcin antibody from cardiac myocytes was the 240-kDa
L-type Ca2+ channel 1 subunit. Anti-sorcin
antibody immunoprecipitated full-length 1 subunits from
cardiac myocytes, C2C12 myotubes, and transfected non-muscle cells
expressing 1 subunits. In contrast, the anti-sorcin antibody did not immunoprecipitate C-terminal truncated forms of
1 subunits that were detected in myotubes. Recombinant
sorcin bound to cardiac and skeletal HIS6-tagged
1 C termini immobilized on Ni2+ resin.
Additionally, anti-sorcin antibody immunoprecipitated C-terminal
fragments of the cardiac 1 subunit exogenously expressed in mammalian cells. The results identified a putative sorcin binding domain within the C terminus of the 1 subunit. These
observations, along with the demonstration that sorcin accumulated
substantially during physiological maturation of the
excitation-contraction coupling apparatus in developing postnatal rat
heart and differentiating C2C12 muscle cells, suggest that sorcin
may mediate interchannel communication during
excitation-contraction coupling in heart and skeletal muscle.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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