期刊
CELL
卷 147, 期 5, 页码 1118-1131出版社
CELL PRESS
DOI: 10.1016/j.cell.2011.10.038
关键词
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资金
- Wellcome Trust
- MRC CDF [G120/952]
- German Science Foundation [SFB 635]
- Medical Research Council [G120/952] Funding Source: researchfish
- MRC [G120/952] Funding Source: UKRI
SNAREs provide a large part of the specificity and energy needed for membrane fusion and, to do so, must be localized to their correct membranes. Here, we show that the R-SNAREs VAMP8, VAMP3, and VAMP2, which cycle between the plasma membrane and endosomes, bind directly to the ubiquitously expressed, PtdIns4, 5P(2)-binding, endocytic clathrin adaptor CALM/PICALM. X-ray crystallography shows that the N-terminal halves of their SNARE motifs bind the CALM(ANTH) domain as helices in a manner that mimics SNARE complex formation. Mutation of residues in the CALM: SNARE interface inhibits binding in vitro and prevents R-SNARE endocytosis in vivo. Thus, CALM: R-SNARE interactions ensure that R-SNAREs, required for the fusion of endocytic clathrin-coated vesicles with endosomes and also for subsequent postendosomal trafficking, are sorted into endocytic vesicles. CALM's role in directing the endocytosis of small R-SNAREs may provide insight into the association of CALM/PICALMmutations with growth retardation, cognitive defects, and Alzheimer's disease.
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