Effects of synaptotagmin binding on SNARE-mediated fusion and trans-SNARE complex formation
| Project/Area Number |
26460297
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
General physiology
|
|---|
| Research Institution | Okayama University |
|---|
Principal Investigator |
Nishiki Teiichi 岡山大学, 医歯薬学総合研究科, 准教授 (70423340)
|
|---|
| Research Collaborator |
FUJINO Kanako
IWAFUJI Ryota
|
|---|
| Project Period (FY) |
2014-04-01 – 2017-03-31
|
| Project Status |
Completed (Fiscal Year 2016)
|
| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
|---|
| Keywords | 神経科学 / 刺激分泌連関 / シナプス小胞 / カルシウムイオン / 開口放出 |
|---|
| Outline of Final Research Achievements |
SNAREs (syntaxin/SNAP-25/synaptobrevin) and synaptotagmin play central roles during Ca2+-dependent neurotransmitter release. In this study, we have studied the effects of synaptotagmin binding on SNARE-mediated fusion and its complex formation. Synaptotagmin stoichiometrically bound to syntaxin in the liposomes containing t-SNAREs (syntaxin, SNAP-25) and dissociated from it by Ca2+. The fusion between synaptobrevin-liposomes and t-SNARE liposomes was inhibited in the presence of synaptotagmin cytoplasmic fragment. This inhibition was reversed by Ca2+. FRET analysis of trans-SNARE complex formation showed that the assembly of SNARE motifs appears to proceed to +6th layers when synaptotagmin binds syntaxin. These results support the idea where synaptotagmin suppresses SNARE-mediated membrane fusion through its syntaxin binding until Ca2+ influx without inhibiting the full assembly of the trans-SNARE complex.
|
Report
(4 results)
Research Products
(2 results)
