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10.1073/pnas.1708492114 http://scihub22266oqcxt.onion/10.1073/pnas.1708492114 C5576828!5576828 !28739947     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28739947 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (34 ): 9110-9115 Nephropedia Template TP {{tp|p=28739947 |t=2017. Morphologies of synaptic protein membrane fusion interfaces |pdf=|usr=}}{{28739947 }} gab.com Text Morphologies of synaptic protein membrane fusion interfaces JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28739947 #FOAvip 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(2+) triggering. We conclude that synaptic proteins have evolved to limit possible contact site assemblies and morphologies to those that promote fast Ca(2+)-triggered release. Twit Text FOAVip Morphologies of synaptic protein membrane fusion interfaces ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28739947 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28739947 #FOAvip English Wikipedia <ref>{{Cite pmid|28739947 }}</ref> Morphologies of synaptic protein membrane fusion interfaces #MMPMID28739947 Gipson P ; Fukuda Y ; Danev R ; Lai Y ; Chen DH ; Baumeister W ; Brunger AT Proc Natl Acad Sci U S A 2017[Aug]; 114 (34 ): 9110-9115 PMID28739947 show ga 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(2+) triggering. We conclude that synaptic proteins have evolved to limit possible contact site assemblies and morphologies to those that promote fast Ca(2+)-triggered release. |*Membrane Fusion [MESH] |Animals [MESH] |Calcium/metabolism [MESH] |Cryoelectron Microscopy/methods [MESH] |Membrane Fusion Proteins/chemistry/*metabolism [MESH] |Models, Molecular [MESH] |Nerve Tissue Proteins/chemistry/metabolism [MESH] |Neurons/*metabolism [MESH] |Protein Binding [MESH] |Protein Domains [MESH] |Proteolipids/metabolism/ultrastructure [MESH] |SNARE Proteins/chemistry/metabolism [MESH] |Synaptic Membranes/*metabolism/ultrastructure [MESH] |Synaptic Vesicles/metabolism/ultrastructure [MESH]Morphologies of synaptic protein membrane fusion interfaces (epmc).pdf DeepDyve Pubget Overpricing