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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2011-5-9
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pubmed:abstractText |
AS160 (TBC1D4) is a known Akt substrate that is phosphorylated downstream of insulin action and that leads to regulated traffic of GLUT4. As GLUT4 vesicle fusion with the plasma membrane is a highly regulated step in GLUT4 traffic, we investigated whether AS160 and 14-3-3 interactions are involved in this process. Fusion was inhibited by a human truncated AS160 variant that encompasses the first N-terminal phosphotyrosine-binding (PTB) domain, by either of the two N-terminal PTB domains, and by a tandem construct of both PTB domains of rat AS160. We also found that in vitro GLUT4 vesicle fusion was strongly inhibited by the 14-3-3-quenching inhibitors R18 and fusicoccin. To investigate the mode of interaction of AS160 and 14-3-3, we examined insulin-dependent increases in the levels of these proteins on GLUT4 vesicles. 14-3-3? was enriched on insulin-stimulated vesicles, and its binding to AS160 on GLUT4 vesicles was inhibited by the AS160 tandem PTB domain construct. These data suggest a model for PTB domain action on GLUT4 vesicle fusion in which these constructs inhibit insulin-stimulated 14-3-3? interaction with AS160 rather than AS160 phosphorylation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-10547847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-11598141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-11994271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-12637568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-14744259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-15169906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-15254270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-15616009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-15866888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-15919790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-15971998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16154100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16154996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16213228,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16762977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16880201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16893906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-16914513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-17189206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-17339344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-17403373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-17617058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-17995453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18039703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18063571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18076383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18325908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18477703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18801932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-18931681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-19046570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-19470471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-19960480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-20220755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-20349035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-20816091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-21195350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-6360220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-8202531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-8349666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-8805370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21454690-9651341
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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/GTPase-Activating 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/LOC686547 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/SLC2A4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/TBC1D4 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1083-351X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16574-82
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21454690-Animals,
pubmed-meshheading:21454690-Cell Membrane,
pubmed-meshheading:21454690-GTPase-Activating Proteins,
pubmed-meshheading:21454690-Glucose,
pubmed-meshheading:21454690-Glucose Transporter Type 4,
pubmed-meshheading:21454690-Humans,
pubmed-meshheading:21454690-Insulin,
pubmed-meshheading:21454690-Phosphorylation,
pubmed-meshheading:21454690-Phosphotyrosine,
pubmed-meshheading:21454690-Protein Binding,
pubmed-meshheading:21454690-Protein Isoforms,
pubmed-meshheading:21454690-Rats
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pubmed:year |
2011
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pubmed:articleTitle |
AS160 phosphotyrosine-binding domain constructs inhibit insulin-stimulated GLUT4 vesicle fusion with the plasma membrane.
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pubmed:affiliation |
Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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