Source:http://linkedlifedata.com/resource/pubmed/id/16857187
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
16
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| pubmed:dateCreated |
2006-9-4
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| pubmed:databankReference | |
| pubmed:abstractText |
The syntrophins are a family of scaffolding proteins with multiple protein interaction domains that link signaling proteins to dystrophin family members. Each of the three most characterized syntrophins (alpha, beta1, beta2) contains a PDZ domain that binds a unique set of signaling proteins including kinases, ion and water channels, and neuronal nitric oxide synthase (nNOS). The PDZ domains of the gamma-syntrophins do not bind nNOS. In vitro pull-down assays show that the gamma-syntrophins can bind dystrophin but have unique preferences for the syntrophin binding sites of dystrophin family members. Despite their ability to bind dystrophin in vitro, neither gamma-syntrophin isoform co-localizes with dystrophin in skeletal muscle. Furthermore, gamma-syntrophins do not co-purify with dystrophin isolated from mouse tissue. These data suggest that the interaction of gamma-syntrophin with dystrophin is transient and potentially subject to regulatory mechanisms. gamma1-Syntrophin is highly expressed in brain and is specifically localized in hippocampal pyramidal neurons, Purkinje neurons in cerebellum, and cortical neurons. gamma2-Syntrophin is expressed in many tissues including skeletal muscle where it is found only in the subsynaptic space beneath the neuromuscular junction. In both neurons and muscle, gamma-syntrophin isoforms localize to the endoplasmic reticulum where they may form a scaffold for signaling and trafficking.
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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/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/syntrophin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0014-4827
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
312
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3084-95
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| pubmed:dateRevised |
2010-12-3
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| pubmed:meshHeading |
pubmed-meshheading:16857187-Amino Acid Sequence,
pubmed-meshheading:16857187-Animals,
pubmed-meshheading:16857187-Antibodies,
pubmed-meshheading:16857187-Dystrophin,
pubmed-meshheading:16857187-Dystrophin-Associated Proteins,
pubmed-meshheading:16857187-Gene Expression Profiling,
pubmed-meshheading:16857187-Humans,
pubmed-meshheading:16857187-Mice,
pubmed-meshheading:16857187-Molecular Sequence Data,
pubmed-meshheading:16857187-Neurons,
pubmed-meshheading:16857187-Nitric Oxide Synthase Type I,
pubmed-meshheading:16857187-Protein Binding,
pubmed-meshheading:16857187-Protein Isoforms,
pubmed-meshheading:16857187-Protein Structure, Tertiary,
pubmed-meshheading:16857187-Protein Transport,
pubmed-meshheading:16857187-Purkinje Cells,
pubmed-meshheading:16857187-Sarcoplasmic Reticulum,
pubmed-meshheading:16857187-Sequence Homology, Amino Acid
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| pubmed:year |
2006
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| pubmed:articleTitle |
gamma-Syntrophin scaffolding is spatially and functionally distinct from that of the alpha/beta syntrophins.
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| pubmed:affiliation |
Department of Physiology and Biophysics, University of Washington, 1959 Pacific ST NE, Seattle, WA 98195-7290, USA.
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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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