Source:http://linkedlifedata.com/resource/pubmed/id/17092484
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2006-11-19
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pubmed:abstractText |
Triadin in the junctional sarcoplasmic reticulum (SR) of skeletal muscle cells has been suggested to interact with ryanodine receptor 1 (RYR1) via its KEKE motifs. Recently, we showed that amino acid residues D4878, D4907, and E4908 in RYR1 are critical for triadin-binding in vitro [J.M. Lee, S.H. Rho, D.W. Shin, C. Cho, W.J. Park, S.H. Eom, J. Ma, D.H. Kim, Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin, J. Biol. Chem. 279 (2004) 6994-7000]. In order to test whether a disruption of the triadin-binding site(s) in RYR1 affects SR Ca(2+) release, alanine-substituted single (D4878A, D4907A, and E4908A) and triple (RYR1-TM) mutants of D4878, D4907, and E4908 were expressed in RYR1-null myotubes. Co-immunoprecipitation experiments showed a 50-60% decrease of triadin brought down in the D4907A and RYR1-TM complexes compared to the triadin-wtRYR1 complex. Ca(2+) imaging experiments using Fluo-4-AM showed atypical caffeine responses in myotubes expressing D4907A and RYR1-TM characterized by either a lack of or slower activation and faster inactivation of Ca(2+) transients. The results suggest that disruption of interaction between triadin and RYR1 impairs RYR1 function and SR Ca(2+) release.
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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/Caffeine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine Receptor Calcium Release...,
http://linkedlifedata.com/resource/pubmed/chemical/triadin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
351
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
909-14
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17092484-Amino Acid Substitution,
pubmed-meshheading:17092484-Animals,
pubmed-meshheading:17092484-Binding Sites,
pubmed-meshheading:17092484-Caffeine,
pubmed-meshheading:17092484-Calcium,
pubmed-meshheading:17092484-Carrier Proteins,
pubmed-meshheading:17092484-Cations, Divalent,
pubmed-meshheading:17092484-Immunoprecipitation,
pubmed-meshheading:17092484-Muscle Fibers, Skeletal,
pubmed-meshheading:17092484-Muscle Proteins,
pubmed-meshheading:17092484-Mutation,
pubmed-meshheading:17092484-Rabbits,
pubmed-meshheading:17092484-Ryanodine Receptor Calcium Release Channel,
pubmed-meshheading:17092484-Sarcoplasmic Reticulum
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pubmed:year |
2006
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pubmed:articleTitle |
Occurrence of atypical Ca2+ transients in triadin-binding deficient-RYR1 mutants.
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pubmed:affiliation |
Department of Physiology, College of Medicine, The Catholic University of Korea, Seoul 137-701, South Korea.
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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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