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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2008-12-17
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pubmed:abstractText |
The skeletal muscle (RyR1) and cardiac muscle (RyR2) ryanodine receptor calcium release channels contain a single, conserved calmodulin (CaM) binding domain, yet are differentially regulated by CaM. Here, we report that high-affinity [(35)S]CaM binding to RyR1 is driven by favorable enthalpic and entropic contributions at Ca(2+) concentrations from <0.01 to 100 microM. At 0.15 microM Ca(2+), [(35)S]CaM bound to RyR2 with decreased affinity and binding enthalpy compared with RyR1. The rates of [(35)S]CaM dissociation from RyR1 increased as the temperature was raised, whereas at 0.15 microM Ca(2+) the rate from RyR2 was little affected. The results suggest major differences in the energetics of CaM binding to and dissociation from RyR1 and RyR2.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-10387100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-10869186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-11274202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-11694536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-11891559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-12185083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-12270947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-12509414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-16274254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-17027503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-2057528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-2434495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-3990807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-6203912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-6346892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-6698971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-7544580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-7552747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-7669888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18618700-9234963
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1097-0134
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pubmed:author |
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pubmed:copyrightInfo |
(c) 2008 Wiley-Liss, Inc.
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pubmed:issnType |
Electronic
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-11
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pubmed:dateRevised |
2011-11-14
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pubmed:meshHeading |
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pubmed:year |
2009
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pubmed:articleTitle |
Thermodynamics of calmodulin binding to cardiac and skeletal muscle ryanodine receptor ion channels.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, USA. meissner@med.unc.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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