SNAREs and traffic.
By W. Hong. Biochimica et Biophysica Acta, 2005
654 citations recorded by the source corpus.
SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) are now generally accepted to be the major players in the final stage of the docking and the subsequent fusion of diverse vesicle-mediated transport events. The SNARE-mediated process is conserved evolutionally from yeast to human, as well as mechanistically and structurally across different transport events in eukaryotic cells. In the post-genomic era, a fairly complete list of "all" SNAREs in several organisms (including human) can now be made. This review aims to summarize the key properties and the mechanism of action of SNAREs in mammalian cells.
Subfields: Cell Biology, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/e732b98c3a39ed295e4191401ddb7a000bcc3f30
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Citations in the corpus
- Retrograde transport from endosomes to the trans-Golgi network (2006, background): “In the simplest model of SNARE function, transport vesicles that bud from the TGN carry specific vesicle-membrane SNAREs (v-SNAREs) that assemble with endosomal target-membrane SNAREs (t-SNAREs) to mediate membrane fusio”
- SNAREs — engines for membrane fusion (2006, background): “For further information, the reader is referred to recent review”
- Membrane Dynamics in the Early Secretory Pathway (2007, background): “These generally have a large cytosolic Nterminal domain containing usually one ca. 65 residue SNARE motif, a transmembrane domain (TMD) with a very short luminal C-terminus, or less frequently a prenyl group (Hong, 2005).”
- The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. (2012, neutral): “These data suggest that Stx17, but not Stx18, is recruited to autophagic membranes.”