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

Tomohiro Yamaguchi, Irina Dulubova, Sang-Won Min, Xiaocheng Chen, Josep Rizo, Thomas C Südhof

Center for Basic Neuroscience, Department of Molecular Genetics, Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA.

Developmental cell 2002 Mar

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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 domain. 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.

Citation

Tomohiro Yamaguchi, Irina Dulubova, Sang-Won Min, Xiaocheng Chen, Josep Rizo, Thomas C Südhof. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Developmental cell. 2002 Mar;2(3):295-305