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PMID: 2581248 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Phosphorylation of the calcium antagonist receptor of the voltage-sensitive calcium channel by cAMP-dependent protein kinase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 82 ·No. 8 ·1985-04-00 ·Pages 2528-32

Curtis BM, Catterall WA

Abstract

Physiological studies indicate that voltage-sensitive calcium channels are regulated by cAMP and protein phosphorylation. The calcium antagonist receptor of the voltage-sensitive calcium channel from transverse-tubule membranes consists of three subunits, designated alpha, beta, and gamma. The catalytic subunit of cAMP-dependent protein kinase phosphorylates both the alpha and beta subunits of the purified receptor at a rate and extent that suggests they are potential physiological substrates of this enzyme. The phosphorylation of the alpha and beta subunits in transverse-tubule membranes was analyzed by two-dimensional gel electrophoresis. In intact transverse-tubule membranes, the alpha subunit is not significantly phosphorylated. However, the beta subunit, identified by its Mr, pI, and binding to wheat germ agglutinin-Sepharose, was one of the substrates selectively phosphorylated by cAMP-dependent protein kinase in transverse-tubule membranes. These results suggest that cAMP-dependent phosphorylation of the beta subunit of the calcium antagonist receptor may be an important regulatory mechanism for calcium channel function.

MeSH Terms
Animals Calcium/metabolism Calcium Channels Electrochemistry In Vitro Techniques Ion Channels/metabolism Kinetics Molecular Weight Muscles/metabolism Phosphorylation Protein Conformation Protein Kinases/metabolism Rabbits Receptors, Nicotinic/isolation & purification,metabolism
Chemicals
Calcium Channels Ion Channels Receptors, Nicotinic Protein Kinases Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Curtis B M
Catterall W A
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33 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.82.8.2528
Published
1985-04-00
Pages
2528-32
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC397592
Subset
IM
Grants
NIGMS NIH HHS · GM07270 · United States
NINDS NIH HHS · NS15751 · United States
External Links
PubMed source DOI: 10.1073/pnas.82.8.2528 PMC Full Text View journal details
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