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 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.
authors.affiliation: Center for Basic Neuroscience, Department of Molecular Genetics, Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA.
authors.forename: Tomohiro
authors.initials: T
authors.lastname: Yamaguchi
authors.forename: Irina
authors.initials: I
authors.lastname: Dulubova
authors.forename: Sang-Won
authors.initials: SW
authors.lastname: Min
authors.forename: Xiaocheng
authors.initials: X
authors.lastname: Chen
authors.forename: Josep
authors.initials: J
authors.lastname: Rizo
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Südhof
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D002522:Chlorocebus aethiops; D017124:Conserved Sequence; D004721:Endoplasmic Reticulum / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D006056:Golgi Apparatus / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary; D050765:Qa-SNARE Proteins; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D020798:Two-Hybrid System Techniques; D014709:Vero Cells; D033921:Vesicular Transport Proteins
chemical_list: D002352:Carrier Proteins; D005656:Fungal Proteins; D008565:Membrane Proteins; D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; C497931:SEC1 protein, S cerevisiae; C072520:SLY1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C077554:Sed5 protein, S cerevisiae; C103868:UFE1 protein, S cerevisiae; D033921:Vesicular Transport Proteins