Functional architecture of an intracellular membrane t-SNARE

Ryoulchi Fukuda, James A. McNew, Thomas Weber, Francesco Parlati, Thomas Engel, Walter Nickel, James E. Rothman, Thomas H. Söllner

Research output: Contribution to journalArticlepeer-review

201 Scopus citations

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.

Original languageEnglish
Pages (from-to)198-202
Number of pages5
JournalNature
Volume407
Issue number6801
DOIs
StatePublished - 14 Sep 2000

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