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dc.contributor.authorSonger, Jennifer A.
dc.contributor.authorMunson, Mary
dc.date2022-08-11T08:09:39.000
dc.date.accessioned2022-08-23T16:39:01Z
dc.date.available2022-08-23T16:39:01Z
dc.date.issued2008-12-17
dc.date.submitted2010-04-06
dc.identifier.citation<p>Mol Biol Cell. 2009 Feb;20(3):973-82. Epub 2008 Dec 10. <a href="http://dx.doi.org/10.1091/mbc.E08-09-0968">Link to article on publisher's site</a></p>
dc.identifier.issn1059-1524 (Linking)
dc.identifier.doi10.1091/mbc.E08-09-0968
dc.identifier.pmid19073882
dc.identifier.urihttp://hdl.handle.net/20.500.14038/39380
dc.description.abstractThe exocyst is an essential protein complex required for targeting and fusion of secretory vesicles to sites of exocytosis at the plasma membrane. To study the function of the exocyst complex, we performed a structure-based mutational analysis of the Saccharomyces cerevisiae exocyst subunit Sec6p. Two "patches" of highly conserved residues are present on the surface of Sec6p; mutation of either patch does not compromise protein stability. Nevertheless, replacement of SEC6 with the patch mutants results in severe temperature-sensitive growth and secretion defects. At nonpermissive conditions, although trafficking of secretory vesicles to the plasma membrane is unimpaired, none of the exocyst subunits are polarized. This is consistent with data from other exocyst temperature-sensitive mutants, which disrupt the integrity of the complex. Surprisingly, however, these patch mutations result in mislocalized exocyst complexes that remain intact. Our results indicate that assembly and polarization of the exocyst are functionally separable events, and that Sec6p is required to anchor exocyst complexes at sites of secretion.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19073882&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2633393/
dc.subjectAlleles
dc.subjectAmino Acid Sequence
dc.subjectAmino Acids
dc.subjectCarrier Proteins
dc.subjectConserved Sequence
dc.subjectExosomes
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectMutant Proteins
dc.subjectMutation
dc.subjectProtein Binding
dc.subjectProtein Subunits
dc.subjectProtein Transport
dc.subjectSaccharomyces cerevisiae
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectVesicular Transport Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSec6p anchors the assembled exocyst complex at sites of secretion
dc.typeJournal Article
dc.source.journaltitleMolecular biology of the cell
dc.source.volume20
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/2177
dc.identifier.contextkey1262957
html.description.abstract<p>The exocyst is an essential protein complex required for targeting and fusion of secretory vesicles to sites of exocytosis at the plasma membrane. To study the function of the exocyst complex, we performed a structure-based mutational analysis of the Saccharomyces cerevisiae exocyst subunit Sec6p. Two "patches" of highly conserved residues are present on the surface of Sec6p; mutation of either patch does not compromise protein stability. Nevertheless, replacement of SEC6 with the patch mutants results in severe temperature-sensitive growth and secretion defects. At nonpermissive conditions, although trafficking of secretory vesicles to the plasma membrane is unimpaired, none of the exocyst subunits are polarized. This is consistent with data from other exocyst temperature-sensitive mutants, which disrupt the integrity of the complex. Surprisingly, however, these patch mutations result in mislocalized exocyst complexes that remain intact. Our results indicate that assembly and polarization of the exocyst are functionally separable events, and that Sec6p is required to anchor exocyst complexes at sites of secretion.</p>
dc.identifier.submissionpathoapubs/2177
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages973-82


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