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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0040715,
umls-concept:C0086597,
umls-concept:C0205314,
umls-concept:C0206131,
umls-concept:C0288881,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C0679622,
umls-concept:C1420175,
umls-concept:C1522702
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pubmed:issue |
6
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pubmed:dateCreated |
1999-7-16
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pubmed:databankReference |
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pubmed:abstractText |
Insulin-stimulated glucose transport and GLUT4 translocation require regulated interactions between the v-SNARE, VAMP2, and the t-SNARE, syntaxin 4. We have isolated a novel syntaxin 4-binding protein, Synip, which specifically interacts with syntaxin 4. Insulin induces a dissociation of the Synip:syntaxin 4 complex due to an apparent decrease in the binding affinity of Synip for syntaxin 4. In contrast, the carboxyterminal domain of Synip does not dissociate from syntaxin 4 in response to insulin stimulation but inhibits glucose transport and GLUT4 translocation. These data implicate Synip as an insulin-regulated syntaxin 4-binding protein directly involved in the control of glucose transport and GLUT4 vesicle translocation.
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pubmed:commentsCorrections |
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
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/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qb-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qc-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SLC2A4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SNAP23 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/STXBP4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Snap23 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Stxbp4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
751-60
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10394363-Adipocytes,
pubmed-meshheading:10394363-Amino Acid Sequence,
pubmed-meshheading:10394363-Animals,
pubmed-meshheading:10394363-Binding, Competitive,
pubmed-meshheading:10394363-Biological Transport,
pubmed-meshheading:10394363-Carrier Proteins,
pubmed-meshheading:10394363-Cell Line,
pubmed-meshheading:10394363-Cloning, Molecular,
pubmed-meshheading:10394363-Cricetinae,
pubmed-meshheading:10394363-Genes, Dominant,
pubmed-meshheading:10394363-Glucose,
pubmed-meshheading:10394363-Glucose Transporter Type 4,
pubmed-meshheading:10394363-Humans,
pubmed-meshheading:10394363-Insulin,
pubmed-meshheading:10394363-Membrane Proteins,
pubmed-meshheading:10394363-Mice,
pubmed-meshheading:10394363-Molecular Sequence Data,
pubmed-meshheading:10394363-Monosaccharide Transport Proteins,
pubmed-meshheading:10394363-Muscle Proteins,
pubmed-meshheading:10394363-Mutation,
pubmed-meshheading:10394363-Organelles,
pubmed-meshheading:10394363-Protein Binding,
pubmed-meshheading:10394363-Qa-SNARE Proteins,
pubmed-meshheading:10394363-Qb-SNARE Proteins,
pubmed-meshheading:10394363-Qc-SNARE Proteins,
pubmed-meshheading:10394363-R-SNARE Proteins,
pubmed-meshheading:10394363-RNA, Messenger,
pubmed-meshheading:10394363-Vesicular Transport Proteins,
pubmed-meshheading:10394363-Yeasts
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pubmed:year |
1999
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pubmed:articleTitle |
Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.
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pubmed:affiliation |
Department of Cell Biology, Parke-Davis Pharmaceutical Research Division, Warner-Lambert Company, Ann Arbor, Michigan 48105, USA.
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pubmed:publicationType |
Journal Article
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