DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lai, Ying | ko |
dc.contributor.author | Lou, Xiaochu | ko |
dc.contributor.author | Jho, Yongseok | ko |
dc.contributor.author | Yoon, Tae-Young | ko |
dc.contributor.author | Shin, Yeon-Kyun | ko |
dc.date.accessioned | 2014-08-29 | - |
dc.date.available | 2014-08-29 | - |
dc.date.created | 2013-12-23 | - |
dc.date.created | 2013-12-23 | - |
dc.date.issued | 2013-11 | - |
dc.identifier.citation | BIOCHEMICAL JOURNAL, v.456, pp.25 - 33 | - |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://hdl.handle.net/10203/188599 | - |
dc.description.abstract | Syt1 (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.language | English | - |
dc.publisher | PORTLAND PRESS LTD | - |
dc.subject | MEMBRANE-FUSION | - |
dc.subject | SNARE COMPLEX | - |
dc.subject | VESICLE FUSION | - |
dc.subject | CA2+ SENSOR | - |
dc.subject | PHOSPHOLIPIDS | - |
dc.subject | EXOCYTOSIS | - |
dc.subject | MECHANISM | - |
dc.subject | DOMAIN | - |
dc.title | The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening | - |
dc.type | Article | - |
dc.identifier.wosid | 000327571300003 | - |
dc.identifier.scopusid | 2-s2.0-84886460455 | - |
dc.type.rims | ART | - |
dc.citation.volume | 456 | - |
dc.citation.beginningpage | 25 | - |
dc.citation.endingpage | 33 | - |
dc.citation.publicationname | BIOCHEMICAL JOURNAL | - |
dc.identifier.doi | 10.1042/BJ20130949 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Yoon, Tae-Young | - |
dc.contributor.nonIdAuthor | Lai, Ying | - |
dc.contributor.nonIdAuthor | Lou, Xiaochu | - |
dc.contributor.nonIdAuthor | Jho, Yongseok | - |
dc.contributor.nonIdAuthor | Shin, Yeon-Kyun | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | bipolar charge distribution | - |
dc.subject.keywordAuthor | Ca2+-dependent content mixing | - |
dc.subject.keywordAuthor | Ca2+-independent docking | - |
dc.subject.keywordAuthor | linker region | - |
dc.subject.keywordAuthor | soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE) | - |
dc.subject.keywordAuthor | synaptotagmin 1 (Syt1) | - |
dc.subject.keywordPlus | MEMBRANE-FUSION | - |
dc.subject.keywordPlus | SNARE COMPLEX | - |
dc.subject.keywordPlus | VESICLE FUSION | - |
dc.subject.keywordPlus | CA2+ SENSOR | - |
dc.subject.keywordPlus | PHOSPHOLIPIDS | - |
dc.subject.keywordPlus | EXOCYTOSIS | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | DOMAIN | - |
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