Munc18 Interacting Proteins

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منابع مشابه

Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.

Sec1/Munc18 (SM) family proteins are essential for every vesicle fusion pathway. The best-characterized SM protein is the synaptic factor Munc18-1, but it remains unclear whether its functions represent conserved mechanisms of SM proteins or specialized activities in neurotransmitter release. To address this question, we dissected Munc18c, a functionally distinct SM protein involved in nonsynap...

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Non-interacting proteins may resemble interacting proteins: prevalence and implications

The vast majority of proteins do not form functional interactions in physiological conditions. We have considered several sets of protein pairs from S. cerevisiae with no functional interaction reported, denoted as non-interacting pairs, and compared their 3D structures to available experimental complexes. We identified some non-interacting pairs with significant structural similarity with expe...

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A role for Sec1/Munc18 proteins in platelet exocytosis.

A critical aspect of haemostasis is the release of clot-forming components from the three intra-platelet stores: dense-core granules, alpha granules and lysosomes. Exocytosis from these granules is mediated by soluble proteins [N-ethylmaleimide-sensitive fusion protein (NSF) and soluble NSF attachment proteins (SNAPs)] and integral membrane proteins [vesicle and target SNAP receptors (v- and t-...

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Selective Activation of Cognate SNAREpins by Sec1/Munc18 (SM) Proteins

Full-length mouse VAMP2-His 6 (pTW2) and the t-SNARE complex between mouse His 6-SNAP-25 and rat syntaxin 1A (pTW34) were expressed and purified as previously described (Melia et al., 2002; Weber et al., 2000). Rat syntaxin 4 and SNAP-23 expression vectors were generated in a similar way as neuronal SNAREs. The proteins were eluted into an OG buffer (25mM HEPES/KOH, pH 7.4, 400 mM KCl, 10% glyc...

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Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins

Sec1/Munc18 (SM) proteins are required for every step of intracellular membrane fusion, but their molecular mechanism of action has been unclear. In this work, we demonstrate a fundamental role of the SM protein: to act as a stimulatory subunit of its cognate SNARE fusion machinery. In a reconstituted system, mammalian SNARE pairs assemble between bilayers to drive a basal fusion reaction. Munc...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2003

ISSN: 0021-9258

DOI: 10.1074/jbc.m301632200