Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif

Tomohiro Yamaguchi, Irina Dulubova, Sang Won Min, Xiaocheng Chen, Jose Rizo-Rey, Thomas C. Südhof

Research output: Contribution to journalArticle

144 Scopus citations

Abstract

Sec1/munc18-like proteins (SM proteins) and SNARE complexes are probably universally required for membrane fusion. However, the molecular mechanism by which they interact has only been defined for synaptic vesicle fusion where munc18 binds to syntaxin in a closed conformation that is incompatible with SNARE complex assembly. We now show that Sly1, an SM protein involved in Golgi and ER fusion, binds to a short, evolutionarily conserved N-terminal peptide of Sed5p and Ufe1p in yeast and of syntaxins 5 and 18 in vertebrates. In these syntaxins, the Sly1 binding peptide is upstream of a separate, autonomously folded N-terminal domainn. These data suggest a potentially general mechanism by which SM proteins could interact with peptides in target proteins independent of core complex assembly and suggest that munc18 binding to syntaxin is an exception.

Original languageEnglish (US)
Pages (from-to)295-305
Number of pages11
JournalDevelopmental Cell
Volume2
Issue number3
DOIs
Publication statusPublished - 2002

    Fingerprint

ASJC Scopus subject areas

  • Developmental Biology

Cite this