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dc.contributor.authorMcNally, James M.
dc.contributor.authorWoodbury, Dixon J.
dc.contributor.authorLemos, Jose R.
dc.date2022-08-11T08:09:01.000
dc.date.accessioned2022-08-23T16:15:48Z
dc.date.available2022-08-23T16:15:48Z
dc.date.issued2004-09-17
dc.date.submitted2008-11-21
dc.identifier.citationCell Biochem Biophys. 2004;41(1):11-24. <a href="http://dx.doi.org/10.1385/CBB:41:1:011 ">Link to article on publisher's site</a>
dc.identifier.issn1085-9195 (Print)
dc.identifier.doi10.1385/CBB:41:1:011
dc.identifier.pmid15371637
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34179
dc.description.abstractThe SNARE complex, involved in vesicular trafficking and exocytosis, is composed of proteins in the vesicular membrane (v-SNAREs) that intertwine with proteins of the target membrane (t-SNAREs). Our results show that modified large dense-core neurosecretory granules (NSGs), isolated from the bovine neurohypophysis, spontaneously fuse with a planar lipid membrane containing only the t-SNARE syntaxin 1A. This provides evidence that syntaxin alone is able to form a functional fusion complex with native v-SNAREs of the NSG. The fusion was similar to constitutive, not regulated, exocytosis because changes in free [Ca2+] had no effect on the syntaxin-mediated fusion. Several deletion mutants of syntaxin 1A were also tested. The removal of the regulatory domain did not significantly reduce spontaneous fusion. However, a syntaxin deletion mutant consisting of only the transmembrane domain was incapable of eliciting spontaneous fusion. Finally, a soluble form of syntaxin 1A (lacking its transmembrane domain) was used to saturate the free syntaxin-binding sites of modified NSGs. This treatment blocks spontaneous fusion of these granules to a bilayer containing full-length syntaxin 1A. This method provides an effective model system to study possible regulatory components affecting vesicle fusion.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15371637&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1385/CBB:41:1:011
dc.subjectLipid Bilayers; Secretory Vesicles; Syntaxin 1
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.subjectNeuroscience and Neurobiology
dc.titleSyntaxin 1A Drives Fusion of Large Dense-Core Neurosecretory Granules Into a Planar Lipid Bilayer
dc.typeJournal Article
dc.source.journaltitleCell biochemistry and biophysics
dc.source.volume41
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/838
dc.identifier.contextkey670494
html.description.abstract<p>The SNARE complex, involved in vesicular trafficking and exocytosis, is composed of proteins in the vesicular membrane (v-SNAREs) that intertwine with proteins of the target membrane (t-SNAREs). Our results show that modified large dense-core neurosecretory granules (NSGs), isolated from the bovine neurohypophysis, spontaneously fuse with a planar lipid membrane containing only the t-SNARE syntaxin 1A. This provides evidence that syntaxin alone is able to form a functional fusion complex with native v-SNAREs of the NSG. The fusion was similar to constitutive, not regulated, exocytosis because changes in free [Ca2+] had no effect on the syntaxin-mediated fusion. Several deletion mutants of syntaxin 1A were also tested. The removal of the regulatory domain did not significantly reduce spontaneous fusion. However, a syntaxin deletion mutant consisting of only the transmembrane domain was incapable of eliciting spontaneous fusion. Finally, a soluble form of syntaxin 1A (lacking its transmembrane domain) was used to saturate the free syntaxin-binding sites of modified NSGs. This treatment blocks spontaneous fusion of these granules to a bilayer containing full-length syntaxin 1A. This method provides an effective model system to study possible regulatory components affecting vesicle fusion.</p>
dc.identifier.submissionpathgsbs_sp/838
dc.contributor.departmentDepartment of Physiology
dc.source.pages11-24
dc.contributor.studentJames McNally


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