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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1997-4-14
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pubmed:abstractText |
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 cAMP-dependent protein kinase-anchoring protein (AKAP). L-type calcium channels purified from rabbit skeletal muscle contain an endogenous co-purifying protein kinase activity that phosphorylates the alpha1 and beta 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 alpha1 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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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6297-302
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9045648-Amino Acid Sequence,
pubmed-meshheading:9045648-Animals,
pubmed-meshheading:9045648-Calcium Channels,
pubmed-meshheading:9045648-Carrier Proteins,
pubmed-meshheading:9045648-Cyclic AMP,
pubmed-meshheading:9045648-Cyclic AMP-Dependent Protein Kinase Type II,
pubmed-meshheading:9045648-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:9045648-Macromolecular Substances,
pubmed-meshheading:9045648-Molecular Sequence Data,
pubmed-meshheading:9045648-Muscle, Skeletal,
pubmed-meshheading:9045648-Peptides,
pubmed-meshheading:9045648-Phosphorylation,
pubmed-meshheading:9045648-Precipitin Tests,
pubmed-meshheading:9045648-Protein Binding,
pubmed-meshheading:9045648-Rabbits
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pubmed:year |
1997
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pubmed:articleTitle |
Identification of a 15-kDa cAMP-dependent protein kinase-anchoring protein associated with skeletal muscle L-type calcium channels.
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pubmed:affiliation |
Department of Pharmacology, University of Washington, Seattle, Washington 98195-7280, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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