2009
DOI: 10.1126/science.1161748
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Membrane Fusion: Grappling with SNARE and SM Proteins

Abstract: The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion. Vesicular and target membrane-localized SNARE proteins zipper up into an α-helical bundle that pulls the two membranes tightly together to exert the force required for fusion. SM proteins, shaped like clasps, bind to trans-SNARE complexes to direct their fusogenic action. Individual fusion reactions are executed by distinct combinations of SNARE a… Show more

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Cited by 1,823 publications
(1,926 citation statements)
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References 73 publications
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“…The soluble part of the SNARE complex consists of four α‐helices (SNARE domains) (Fasshauer et al , 1998; Sutton et al , 1998; Südhof & Rothman, 2009). Surprisingly, the phosphorylation sites in VAMP8 that we identified face the 3 other α‐helices of the SNARE complex (Fig 2A) (Fasshauer et al , 1998; Sutton et al , 1998; Diao et al , 2015) as part of the 16 conserved SNARE layers (Fasshauer et al , 1998) that are buried inside the SNARE complex (T47 at layer +3, S54 at layer +5, and T53 close to layer +5) (Figs 2B–D and EV2C).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The soluble part of the SNARE complex consists of four α‐helices (SNARE domains) (Fasshauer et al , 1998; Sutton et al , 1998; Südhof & Rothman, 2009). Surprisingly, the phosphorylation sites in VAMP8 that we identified face the 3 other α‐helices of the SNARE complex (Fig 2A) (Fasshauer et al , 1998; Sutton et al , 1998; Diao et al , 2015) as part of the 16 conserved SNARE layers (Fasshauer et al , 1998) that are buried inside the SNARE complex (T47 at layer +3, S54 at layer +5, and T53 close to layer +5) (Figs 2B–D and EV2C).…”
Section: Resultsmentioning
confidence: 99%
“…These regulated vesicle fusion events are typically much slower than the Ca 2+ ‐triggered release of synaptic vesicles (Wickner & Schekman, 2008; Südhof & Rothman, 2009; Jahn & Fasshauer, 2012; Wollman & Meyer, 2012; Südhof, 2013) and require in addition to SNARE proteins signaling regulators such as protein kinase C (PKC) (Oancea & Meyer, 1998; Nechushtan et al , 2000; Newton, 2010). Despite decades of investigation, the role of PKC in vesicle secretion remains incompletely resolved (Nishizuka, 1986; Leitges et al , 1996; Kalesnikoff & Galli, 2008; Lorentz et al , 2012), but may involve incoherent feed‐forward regulation (Mangan & Alon, 2003) as PKC is known to both activate (Nechushtan et al , 2000; Newton, 2010) and suppress (McHugh et al , 2000; Leitges et al , 2002; Bousquet et al , 2010) numerous cell responses.…”
Section: Introductionmentioning
confidence: 99%
“…It became apparent that most disease-causing proteins possess isoforms that have an important role in synaptic transmission from neurons and neuroendocrine cells 11,23,25 . As the molecular mechanisms leading to synaptic transmission have been studied in great detail 26,27 , it was assumed that, for example, syntaxin11, the defective protein in FHL4, functions as a t-SNARE mediating the fusion of LGs with the plasma membrane 23 . However, SNARE complexes function in a large variety of intracellular membrane fusion reactions 1,2 .…”
Section: Discussionmentioning
confidence: 99%
“…SNAP-25 (synaptosomal-associated protein of 25 kDa) is a SNARE protein that participates in the regulation of synapticvesicle (SV) exocytosis [1][2][3] and negatively modulates voltagegated ion channels (VGCCs) [4][5][6][7]. Consistently, silencing endogenous SNAP-25 results in increased VGCC activity in glutamatergic neurons [8,9].…”
Section: Introductionmentioning
confidence: 99%