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dc.contributor.authorSleeman, Mark W.
dc.contributor.authorDonegan, Niles P.
dc.contributor.authorHeller-Harrison, Robin A.
dc.contributor.authorLane, William S.
dc.contributor.authorCzech, Michael P.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:09Z
dc.date.available2022-08-23T16:54:09Z
dc.date.issued1998-03-07
dc.date.submitted2008-08-04
dc.identifier.citation<p>J Biol Chem. 1998 Feb 6;273(6):3132-5.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.273.6.3132
dc.identifier.pmid9452420
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42433
dc.description.abstractGLUT4, the glucose transporter present in insulin-sensitive tissues, resides in intracellular vesicular structures and translocates to the cell surface in response to insulin. In an attempt to identify proteins present in these structures, GLUT4-enriched vesicles prepared from rat adipocytes treated with or without insulin were prepared by sucrose velocity gradient centrifugation and immunoadsorbed with anti-GLUT4 antibody. We report here the sequence identification by high performance liquid chromatography-ion trap mass spectrometry of a p75 protein band, long chain acyl-CoA synthetase-1, specifically present in immunoadsorbed GLUT4-containing vesicles but not in vesicles adsorbed by nonimmune serum. Acyl-CoA synthetase activity detected in GLUT4-enriched vesicles prepared by gradient centrifugation from insulin-treated adipocytes was decreased to about the same extent as GLUT4 protein. Additionally, immunoadsorbed GLUT4 vesicles were found to catalyze palmitoylation of proteins when incubated with labeled palmitate, a pathway that requires palmitate esterification with CoA. These data indicate that the insulin-sensitive membrane compartment that sequesters GLUT4 in fat cells contains long chain acyl-CoA synthetase-1 and its product fatty acyl-CoA, shown previously to be required for budding and fusion in membrane trafficking processes.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9452420&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.273.6.3132
dc.subjectAcyl Coenzyme A
dc.subjectAdipocytes
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCoenzyme A Ligases
dc.subjectGlucose Transporter Type 4
dc.subjectMale
dc.subjectMembrane Fusion
dc.subjectMicroscopy, Electron
dc.subjectMonosaccharide Transport Proteins
dc.subject*Muscle Proteins
dc.subjectRats
dc.subjectRats, Sprague-Dawley
dc.subject*Repressor Proteins
dc.subject*Saccharomyces cerevisiae Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleAssociation of acyl-CoA synthetase-1 with GLUT4-containing vesicles
dc.typeArticle
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume273
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/783
dc.identifier.contextkey564698
html.description.abstract<p>GLUT4, the glucose transporter present in insulin-sensitive tissues, resides in intracellular vesicular structures and translocates to the cell surface in response to insulin. In an attempt to identify proteins present in these structures, GLUT4-enriched vesicles prepared from rat adipocytes treated with or without insulin were prepared by sucrose velocity gradient centrifugation and immunoadsorbed with anti-GLUT4 antibody. We report here the sequence identification by high performance liquid chromatography-ion trap mass spectrometry of a p75 protein band, long chain acyl-CoA synthetase-1, specifically present in immunoadsorbed GLUT4-containing vesicles but not in vesicles adsorbed by nonimmune serum. Acyl-CoA synthetase activity detected in GLUT4-enriched vesicles prepared by gradient centrifugation from insulin-treated adipocytes was decreased to about the same extent as GLUT4 protein. Additionally, immunoadsorbed GLUT4 vesicles were found to catalyze palmitoylation of proteins when incubated with labeled palmitate, a pathway that requires palmitate esterification with CoA. These data indicate that the insulin-sensitive membrane compartment that sequesters GLUT4 in fat cells contains long chain acyl-CoA synthetase-1 and its product fatty acyl-CoA, shown previously to be required for budding and fusion in membrane trafficking processes.</p>
dc.identifier.submissionpathoapubs/783
dc.contributor.departmentProgram in Molecular Medicine and the Department of Biochemistry and Molecular Biology
dc.source.pages3132-5


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