Results 1 to 10 of about 491 (116)
Mechanistic insights into the recycling machine of the SNARE complex [PDF]
Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual
Minglei Zhao +2 more
exaly +4 more sources
Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly
Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction between Munc13-1 and synaptobrevin-2 that is critical for the transition of the Munc18-1/syntaxin-1 ...
Shen Wang +6 more
doaj +2 more sources
One SNARE complex is sufficient for membrane fusion [PDF]
In eukaryotes, most intracellular membrane fusion reactions are mediated by the interaction of SNARE proteins that are present in both fusing membranes. However, the minimal number of SNARE complexes needed for membrane fusion is not known. Here we show unambiguously that one SNARE complex is sufficient for membrane fusion.
Geert Van Den Bogaart +2 more
exaly +5 more sources
SNARE Complexity in Arbuscular Mycorrhizal Symbiosis [PDF]
How cells control the proper delivery of vesicles and their associated cargo to specific plasma membrane (PM) domains upon internal or external cues is a major question in plant cell biology. A widely held hypothesis is that expansion of plant exocytotic machinery components, such as SNARE proteins, has led to a diversification of exocytotic membrane ...
Huisman, Rik +3 more
openaire +4 more sources
Action of Complexin on SNARE Complex [PDF]
Calcium-dependent synaptic vesicle exocytosis requires three SNARE (soluble N-ethylmaleimide-sensitive-factor attachment protein receptor) proteins: synaptobrevin/vesicle-associated membrane protein in the vesicular membrane and syntaxin and SNAP-25 in the presynaptic membrane.
Kuang, Hu +3 more
openaire +2 more sources
SNARE complex assembly and disassembly [PDF]
A fundamental hallmark of eukaryotic cells is their compartmentalization into functionally distinct organelles, including those of the secretory and endocytic pathways. Transport of cargo between these compartments and to/from the cell surface is mediated by membrane-bound vesicles and tubules.
Tae-Young, Yoon, Mary, Munson
openaire +2 more sources
Sequential analysis of trans-SNARE formation in intracellular membrane fusion. [PDF]
SNARE complexes are required for membrane fusion in the endomembrane system. They contain coiled-coil bundles of four helices, three (Q(a), Q(b), and Q(c)) from target (t)-SNAREs and one (R) from the vesicular (v)-SNARE.
Kannan Alpadi +7 more
doaj +1 more source
Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs.
Hongki Song +4 more
doaj +1 more source
Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion [PDF]
SNARE functions during membrane docking and fusion are regulated by Sec1/Munc18 (SM) chaperones and Rab/Ypt GTPase effectors. These functions for yeast vacuole fusion are combined in the six-subunit HOPS complex. HOPS facilitates Ypt7p nucleotide exchange, is a Ypt7p effector, and contains an SM protein.
Kevin M, Collins +3 more
openaire +2 more sources
News and Views into the SNARE Complexity in Arabidopsis [PDF]
Secretory organelles are engaged in a continuous flux of membranes, which is believed to occur mostly via transport vesicles. Being critical in maintaining several cellular functions, transport vesicles are membrane-enclosed sacs that temporarily store and then deliver membrane lipids, protein, and polysaccharides. SNAREs have a crucial role in vesicle
Sang-Jin eKim +4 more
openaire +3 more sources

