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-Structure paper
タイトル | Morphologies of synaptic protein membrane fusion interfaces. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 114, Issue 34, Page 9110-9115, Year 2017 |
掲載日 | 2017年8月22日 |
著者 | Preeti Gipson / Yoshiyuki Fukuda / Radostin Danev / Ying Lai / Dong-Hua Chen / Wolfgang Baumeister / Axel T Brunger / |
PubMed 要旨 | Neurotransmitter release is orchestrated by synaptic proteins, such as SNAREs, synaptotagmin, and complexin, but the molecular mechanisms remain unclear. We visualized functionally active synaptic ...Neurotransmitter release is orchestrated by synaptic proteins, such as SNAREs, synaptotagmin, and complexin, but the molecular mechanisms remain unclear. We visualized functionally active synaptic proteins reconstituted into proteoliposomes and their interactions in a native membrane environment by electron cryotomography with a Volta phase plate for improved resolvability. The images revealed individual synaptic proteins and synaptic protein complex densities at prefusion contact sites between membranes. We observed distinct morphologies of individual synaptic proteins and their complexes. The minimal system, consisting of neuronal SNAREs and synaptotagmin-1, produced point and long-contact prefusion states. Morphologies and populations of these states changed as the regulatory factors complexin and Munc13 were added. Complexin increased the membrane separation, along with a higher propensity of point contacts. Further inclusion of the priming factor Munc13 exclusively restricted prefusion states to point contacts, all of which efficiently fused upon Ca triggering. We conclude that synaptic proteins have evolved to limit possible contact site assemblies and morphologies to those that promote fast Ca-triggered release. |
リンク | Proc Natl Acad Sci U S A / PubMed:28739947 / PubMed Central |
手法 | EM (トモグラフィー) |
構造データ | EMDB-8807: EMDB-8808: EMDB-8809: EMDB-8810: EMDB-8811: |
由来 |
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