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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1995-4-14
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pubmed:abstractText |
Syntrophin represents three cytoplasmic components of the dystrophin-glycoprotein complex that links the cytoskeleton to the extracellular matrix in skeletal muscle. alpha-Syntrophin has now been translated in vitro and shown to associate directly with all three components of the syntrophin triplet and with dystrophin. The in vitro translated 71-kDa non-muscle dystrophin isoform, containing the cystein-rich/C-terminal domain, can also interact with the syntrophin triplet. The syntrophin binding motif in dystrophin was localized to exons 73 and 74 including amino acids 3447-3481 by comparing the interactions of alpha-syntrophin and seven overlapping human dystrophin fusion proteins. More than one syntrophin interaction site in this binding motif was suggested. alpha-Syntrophin also interacts directly with a C-terminal utrophin fusion protein. alpha-Syntrophin is localized to the muscle sarcolemma as well as to the neuromuscular junction in control mouse muscle. However, similar to utrophin, alpha-syntrophin is only present at the neuromuscular junction in mdx mouse muscle in which dystrophin is absent. Our data suggest that alpha-syntrophin binds all syntrophin isoforms, and syntrophin directly interacts with dystrophin through more than one binding site in dystrophin exons 73 and 74 including amino acids 3447-3481.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Utrn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Utrophin,
http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/syntrophin alpha1
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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 |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4975-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7890602-ATP-Binding Cassette Transporters,
pubmed-meshheading:7890602-Amino Acid Sequence,
pubmed-meshheading:7890602-Animals,
pubmed-meshheading:7890602-Bacterial Proteins,
pubmed-meshheading:7890602-Base Sequence,
pubmed-meshheading:7890602-Binding Sites,
pubmed-meshheading:7890602-Calcium-Binding Proteins,
pubmed-meshheading:7890602-Carrier Proteins,
pubmed-meshheading:7890602-Cytoskeletal Proteins,
pubmed-meshheading:7890602-DNA Primers,
pubmed-meshheading:7890602-Dystrophin,
pubmed-meshheading:7890602-Escherichia coli,
pubmed-meshheading:7890602-Escherichia coli Proteins,
pubmed-meshheading:7890602-Exons,
pubmed-meshheading:7890602-Glutathione Transferase,
pubmed-meshheading:7890602-Humans,
pubmed-meshheading:7890602-Maltose-Binding Proteins,
pubmed-meshheading:7890602-Membrane Proteins,
pubmed-meshheading:7890602-Molecular Sequence Data,
pubmed-meshheading:7890602-Monosaccharide Transport Proteins,
pubmed-meshheading:7890602-Muscle Proteins,
pubmed-meshheading:7890602-Muscles,
pubmed-meshheading:7890602-Polymerase Chain Reaction,
pubmed-meshheading:7890602-Protein Biosynthesis,
pubmed-meshheading:7890602-Rabbits,
pubmed-meshheading:7890602-Recombinant Fusion Proteins,
pubmed-meshheading:7890602-Transcription, Genetic,
pubmed-meshheading:7890602-Utrophin
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pubmed:year |
1995
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pubmed:articleTitle |
Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin.
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pubmed:affiliation |
Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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