An electrostatically preferred lateral orientation of SNARE complex suggests novel mechanisms for driving membrane fusion. [PDF]
PLoS ONE, 2010 Biological membrane fusion is a basic cellular process catalyzed by SNARE proteins and additional auxiliary factors. Yet, the critical mechanistic details of SNARE-catalyzed membrane fusion are poorly understood, especially during rapid synaptic ...
Ting Guo, Lin-Chen Gong, Sen-Fang Sui
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A model for the self-organization of vesicular flux and protein distributions in the Golgi apparatus [PDF]
, 2013 The generation of two non-identical membrane compartments via exchange of vesicles is considered to require two types of vesicles specified by distinct cytosolic coats that selectively recruit cargo and two membrane-bound SNARE pairs that specify fusion ...
Ispolatov, Iaroslav, Muesch, Anne
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Analysis of SEC9 suppression reveals a relationship of SNARE function to cell physiology. [PDF]
PLoS ONE, 2009 BACKGROUND:Growth and division of Saccharomyces cerevisiae is dependent on the action of SNARE proteins that are required for membrane fusion. SNAREs are regulated, through a poorly understood mechanism, to ensure membrane fusion at the correct time and ...
Daniel C Williams, Peter J Novick
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LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate [PDF]
, 2016 Background Lrrk2, a gene linked to Parkinson\u2019s disease, encodes a large scaffolding protein with kinase and GTPase activities implicated in vesicle and cytoskeletal-related processes.
Arrigoni, Giorgio +15 more
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Snake and spider toxins induce a rapid recovery of function of botulinum neurotoxin paralysed neuromuscular junction [PDF]
, 2015 Botulinum neurotoxins (BoNTs) and some animal neurotoxins (-Bungarotoxin, -Btx, from elapid snakes and -Latrotoxin, -Ltx, from black widow spiders) are pre-synaptic neurotoxins that paralyse motor axon terminals with similar clinical outcomes in patients.
Duregotti, Elisa +6 more
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Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion. [PDF]
, 2012 The molecular underpinnings of synaptic vesicle fusion for fast neurotransmitter release are still unclear. Here, we used a single vesicle-vesicle system with reconstituted SNARE and synaptotagmin-1 proteoliposomes to decipher the temporal sequence of ...
Brunger, Axel T +13 more
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NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin
eLife, 2018 SNARE complex disassembly by the ATPase NSF is essential for neurotransmitter release and other membrane trafficking processes. We developed a single-molecule FRET assay to monitor repeated rounds of NSF-mediated disassembly and reassembly of individual ...
Ucheor B Choi +6 more
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Epileptic Phenotypes Associated With SNAREs and Related Synaptic Vesicle Exocytosis Machinery
Frontiers in Neurology, 2022 SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptor) are an heterogeneous family of proteins that, together with their key regulators, are implicated in synaptic vesicle exocytosis and synaptic transmission. SNAREs represent the
Elisa Cali +3 more
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Molecular Dynamics Simulations of SNARE Complex Unzipping [PDF]
Biophysical Journal, 2014 The SNARE proteins facilitate biological membrane fusion. The neuronal SNARE proteins, namely VAMP-2, also called synaptobrevin 2, SNAP-25, and syntaxin-1A together form a coiled-coil complex. The formation of this SNARE complex is vital for vesicle-plasma membrane fusion resulting in neurotransmitter exocytosis.
Satyan Sharma, Manfred Lindau
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Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion. [PDF]
PLoS Genetics, 2018 The autophagosomal SNARE Syntaxin17 (Syx17) forms a complex with Snap29 and Vamp7/8 to promote autophagosome-lysosome fusion via multiple interactions with the tethering complex HOPS.
Szabolcs Takáts +7 more
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