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

doi:10.1016/S1534-5807(02)00125-9

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 journal › Article › peer-review

156 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 language	English (US)
Pages (from-to)	295-305
Number of pages	11
Journal	Developmental cell
Volume	2
Issue number	3
DOIs	https://doi.org/10.1016/S1534-5807(02)00125-9
State	Published - 2002

ASJC Scopus subject areas

Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Developmental Biology
Cell Biology

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10.1016/S1534-5807(02)00125-9

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title = "Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif",

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.",

author = "Tomohiro Yamaguchi and Irina Dulubova and Min, {Sang Won} and Xiaocheng Chen and Jose Rizo-Rey and S{\"u}dhof, {Thomas C.}",

note = "Funding Information: We thank Dr. H. Kramer (Dallas) for providing Vero cells and antibodies, Drs. R. Scheller, D. James, and Dr. B. Horazdovsky for cDNA clones and yeast genomic DNA, and Drs. G. Warren and V. Malhotra for helpful comments. We are grateful to Ms. I. Leznicki, I. Huryeva, A. Roth, Y. Gao, and E. Borowicz for excellent technical assistance. This study was supported by grant NS37200 from the National Institutes of Health to J.R. and by a fellowship from the Japan Society for the Promotion of Science to T.Y.",

year = "2002",

doi = "10.1016/S1534-5807(02)00125-9",

language = "English (US)",

volume = "2",

pages = "295--305",

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AU - Yamaguchi, Tomohiro

AU - Dulubova, Irina

AU - Min, Sang Won

AU - Chen, Xiaocheng

AU - Rizo-Rey, Jose

AU - Südhof, Thomas C.

N1 - Funding Information: We thank Dr. H. Kramer (Dallas) for providing Vero cells and antibodies, Drs. R. Scheller, D. James, and Dr. B. Horazdovsky for cDNA clones and yeast genomic DNA, and Drs. G. Warren and V. Malhotra for helpful comments. We are grateful to Ms. I. Leznicki, I. Huryeva, A. Roth, Y. Gao, and E. Borowicz for excellent technical assistance. This study was supported by grant NS37200 from the National Institutes of Health to J.R. and by a fellowship from the Japan Society for the Promotion of Science to T.Y.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

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

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