The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening

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dc.contributor.authorLai, Yingko
dc.contributor.authorLou, Xiaochuko
dc.contributor.authorJho, Yongseokko
dc.contributor.authorYoon, Tae-Youngko
dc.contributor.authorShin, Yeon-Kyunko
dc.date.accessioned2014-08-29-
dc.date.available2014-08-29-
dc.date.created2013-12-23-
dc.date.created2013-12-23-
dc.date.issued2013-11-
dc.identifier.citationBIOCHEMICAL JOURNAL, v.456, pp.25 - 33-
dc.identifier.issn0264-6021-
dc.identifier.urihttp://hdl.handle.net/10203/188599-
dc.description.abstractSyt1 (synaptotagmin 1), a major Ca2+ sensor for fast neurotransmitter release, contains tandem Ca2+-binding C2 domains (C2AB), a single transmembrane alpha-helix and a highly charged 60-residue-long linker in between. Using single-vesicle-docking and content-mixing assays we found that the linker region of Syt1 is essential for its two signature functions: Ca2+-independent vesicle docking and Ca2+-dependent fusion pore opening. The linker contains the basic-amino-acid-rich N-terminal region and the acidic-amino-acid-rich C-terminal region. When the charge segregation was disrupted, fusion pore opening was slowed, whereas docking was unchanged. Intramolecular disulfide cross-linking between N- and C-terminal regions of the linker or deletion of 40 residues from the linker reduced docking while enhancing pore opening, although the changes were subtle. EPR analysis showed Ca2+-induced line broadening reflecting a conformational change in the linker region. Thus the results of the present study suggest that the electrostatically bipartite linker region may extend for docking and fold to facilitate pore opening.-
dc.languageEnglish-
dc.publisherPORTLAND PRESS LTD-
dc.subjectMEMBRANE-FUSION-
dc.subjectSNARE COMPLEX-
dc.subjectVESICLE FUSION-
dc.subjectCA2+ SENSOR-
dc.subjectPHOSPHOLIPIDS-
dc.subjectEXOCYTOSIS-
dc.subjectMECHANISM-
dc.subjectDOMAIN-
dc.titleThe synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening-
dc.typeArticle-
dc.identifier.wosid000327571300003-
dc.identifier.scopusid2-s2.0-84886460455-
dc.type.rimsART-
dc.citation.volume456-
dc.citation.beginningpage25-
dc.citation.endingpage33-
dc.citation.publicationnameBIOCHEMICAL JOURNAL-
dc.identifier.doi10.1042/BJ20130949-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorYoon, Tae-Young-
dc.contributor.nonIdAuthorLai, Ying-
dc.contributor.nonIdAuthorLou, Xiaochu-
dc.contributor.nonIdAuthorJho, Yongseok-
dc.contributor.nonIdAuthorShin, Yeon-Kyun-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorbipolar charge distribution-
dc.subject.keywordAuthorCa2+-dependent content mixing-
dc.subject.keywordAuthorCa2+-independent docking-
dc.subject.keywordAuthorlinker region-
dc.subject.keywordAuthorsoluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE)-
dc.subject.keywordAuthorsynaptotagmin 1 (Syt1)-
dc.subject.keywordPlusMEMBRANE-FUSION-
dc.subject.keywordPlusSNARE COMPLEX-
dc.subject.keywordPlusVESICLE FUSION-
dc.subject.keywordPlusCA2+ SENSOR-
dc.subject.keywordPlusPHOSPHOLIPIDS-
dc.subject.keywordPlusEXOCYTOSIS-
dc.subject.keywordPlusMECHANISM-
dc.subject.keywordPlusDOMAIN-
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