Functional architecture of an intracellular membrane t-SNARE Journal Article
| Authors: | Fukuda, R.; Mcnew, J. A.; Weber, T.; Parlati, F.; Engel, T.; Nickel, W.; Rothman, J. E.; Söllner, T. H. |
| Article Title: | Functional architecture of an intracellular membrane t-SNARE |
| Abstract: | Lipid bilayer fusion is mediated by SNAREs (soluble N-ethyl-maleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, of which one is supplied by the v-SNARE and the other three by the t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and a SNAP-25 protein contributes the other two. Although there are numerous homologues of syntaxin on intracellular membranes, there are only two SNAP-25-related proteins in yeast, Sec9 and Spo20, both of which are localized to the plasma membrane and function in secretion and sporulation, respectively. What replaces SNAP-25 in t-SNAREs of intracellular membranes? Here we show that an intracellular t-SNARE is built from a 'heavy chain' homologous to syntaxin and two separate non-syntaxin 'light chains'. SNAP-25 may thus be the exception rather than the rule, having been derived from genes that encoded separate light chains that fused during evolution to produce a single gene encoding one protein with two helices. |
| Keywords: | nonhuman; protein conformation; protein analysis; protein protein interaction; nerve tissue proteins; protein binding; membrane proteins; recombinant fusion proteins; saccharomyces cerevisiae; escherichia coli; cell membrane; saccharomyces cerevisiae proteins; protein structure; protein structure, quaternary; fungal proteins; vesicular transport proteins; intracellular membranes; membrane structure; snare protein; qa-snare proteins; r-snare proteins; snare proteins; synaptosomal-associated protein 25; priority journal; article |
| Journal Title: | Nature |
| Volume: | 407 |
| Issue: | 6801 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2000-09-14 |
| Start Page: | 198 |
| End Page: | 202 |
| Language: | English |
| DOI: | 10.1038/35025084 |
| PUBMED: | 11001059 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 18 November 2015 -- Source: Scopus |
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