Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Carrier Proteins, Cercopithecus aethiops, Conserved Sequence, Endoplasmic Reticulum, Evolution, Molecular, Fungal Proteins, Golgi Apparatus, Membrane Proteins, Molecular Sequence Data, Munc18 Proteins, Nerve Tissue Proteins, Protein Structure, Tertiary, Qa-SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Vero Cells, Vesicular Transport Proteins
Amino Acid Sequence, Animals, Carrier Proteins, Cercopithecus aethiops, Conserved Sequence, Endoplasmic Reticulum, Evolution, Molecular, Fungal Proteins, Golgi Apparatus, Membrane Proteins, Molecular Sequence Data, Munc18 Proteins, Nerve Tissue Proteins, Protein Structure, Tertiary, Qa-SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Vero Cells, Vesicular Transport Proteins
Dev. Cell
Date: Mar. 01, 2002
PubMed ID: 11879635
View in: Pubmed Google Scholar
Download Curated Data For This Publication
17566
Switch View:
- Interactions 5