Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion
نویسندگان
چکیده
منابع مشابه
Sec1p directly stimulates SNARE-mediated membrane fusion in vitro
Sec1 proteins are critical players in membrane trafficking, yet their precise role remains unknown. We have examined the role of Sec1p in the regulation of post-Golgi secretion in Saccharomyces cerevisiae. Indirect immunofluorescence shows that endogenous Sec1p is found primarily at the bud neck in newly budded cells and in patches broadly distributed within the plasma membrane in unbudded cell...
متن کاملCalcium drives fusion of SNARE-apposed bilayers.
N-ethylmalemide-sensitive factor attachment protein receptor (SNARE) has been proposed to play a critical role in the membrane fusion process. The SNARE complex was suggested to be the minimal fusion machinery. However, there is mounting evidence for a major role of calcium in membrane fusion. Hence, the role of calcium in SNARE-induced membrane fusion was the focus of this study. It revealed t...
متن کاملPhosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion
Phosphatidylinositol 4,5-bisphosphate (PI 4,5-P(2)) on the plasma membrane is essential for vesicle exocytosis but its role in membrane fusion has not been determined. Here, we quantify the concentration of PI 4,5-P(2) as approximately 6 mol% in the cytoplasmic leaflet of plasma membrane microdomains at sites of docked vesicles. At this concentration of PI 4,5-P(2) soluble NSF attachment protei...
متن کاملMunc13-4 reconstitutes calcium-dependent SNARE-mediated membrane fusion
Munc13-4 is a widely expressed member of the CAPS/Munc13 protein family proposed to function in priming secretory granules for exocytosis. Munc13-4 contains N- and C-terminal C2 domains (C2A and C2B) predicted to bind Ca(2+), but Ca(2+)-dependent regulation of Munc13-4 activity has not been described. The C2 domains bracket a predicted SNARE-binding domain, but whether Munc13-4 interacts with S...
متن کاملReconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones.
The homotypic fusion of yeast vacuoles, each with 3Q- and 1R-SNARE, requires SNARE chaperones (Sec17p/Sec18p and HOPS) and regulatory lipids (sterol, diacylglycerol and phosphoinositides). Pairs of liposomes of phosphatidylcholine/phosphatidylserine, bearing three vacuolar Q-SNAREs on one and the R-SNARE on the other, undergo slow lipid mixing, but this is unaffected by HOPS and inhibited by Se...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2006
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0606881103