Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p. 2006

John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
Department of Pathology and Laboratory Medicine, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.

The Sec1/Munc-18 (SM) family of proteins is required for vesicle fusion in eukaryotic cells and has been linked to the membrane-fusion proteins known as soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). SM proteins may activate the target-membrane SNARE, syntaxin, for assembly into the fusogenic SNARE complex. In support of an activation role, SM proteins bind directly to their cognate syntaxins. An exception is the yeast Sec1p, which does not bind the yeast plasma-membrane syntaxin, Sso1p. This exception could be explained if the SM interaction motif were blocked by the highly stable closed conformation of Sso1p. We tested the possibility of a latent binding motif using sso1 mutants in yeast and reconstituted the Sec1p binding specificity observed in vivo with purified proteins in vitro. Our results indicate there is no latent binding motif in Sso1p. Instead, Sec1p binds specifically to the ternary SNARE complex, with no detectable binding to the binary t-SNARE complex or any of the three individual SNAREs in their uncomplexed forms. We propose that vesicle fusion requires a specific interaction between the SM protein and the ternary SNARE complex.

UI MeSH Term Description Entries
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D046912 Multiprotein Complexes Macromolecular complexes formed from the association of defined protein subunits. Macromolecular Protein Complexes,Complexes, Macromolecular Protein,Complexes, Multiprotein,Protein Complexes, Macromolecular
D050600 SNARE Proteins A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.) SNAP Receptor,SNARE Protein,NSF Attachment Protein Receptor,Receptor, SNAP,SNAP Receptors,SNARE,SNAREs,Soluble N-ethylmaleimide-Sensitive-Factor Attachment Protein Receptor,Target Membrane SNARE Proteins,Target SNARE Proteins,Vesicle SNARE Proteins,Vesicular SNARE Proteins,t-SNARE,tSNAREs,v-SNARE,v-SNAREs,Protein, SNARE,SNARE Proteins, Target,SNARE Proteins, Vesicle,SNARE Proteins, Vesicular,Soluble N ethylmaleimide Sensitive Factor Attachment Protein Receptor,v SNAREs
D050765 Qa-SNARE Proteins A subfamily of Q-SNARE PROTEINS which occupy the same position as syntaxin 1A in the SNARE complex and which also are most similar to syntaxin 1A in their AMINO ACID SEQUENCE. This subfamily is also known as the syntaxins, although a few so called syntaxins are Qc-SNARES. Qa-SNAREs,Syntaxin,Syntaxin 10,Syntaxin 10 Protein,Syntaxin 11,Syntaxin 11 Protein,Syntaxin 13,Syntaxin 13 Protein,Syntaxin 17,Syntaxin 17 Protein,Syntaxin 18,Syntaxin 18 Protein,Syntaxin 1A Homologs,Syntaxin 3,Syntaxin 3 Protein,Syntaxin 3A,Syntaxin 3A Protein,Syntaxin 3B,Syntaxin 3B Protein,Syntaxin 3C,Syntaxin 3C Protein,Syntaxin 3D,Syntaxin 3D Protein,Syntaxin 4,Syntaxin 4 Protein,Syntaxin 5,Syntaxin 5 Protein,Syntaxin 6,Syntaxin 6 Protein,Syntaxin 7,Syntaxin 7 Protein,Syntaxin 8,Syntaxin 8 Protein,Syntaxin Protein,Syntaxin Proteins,Syntaxins,Protein, Syntaxin,Protein, Syntaxin 11,Proteins, Syntaxin,Qa SNARE Proteins,Qa SNAREs
D051938 Munc18 Proteins A family of proteins involved in intracellular membrane trafficking. They interact with SYNTAXINS and play important roles in vesicular docking and fusion during EXOCYTOSIS. Their name derives from the fact that they are related to Unc-18 protein, C elegans. Munc-18 Proteins,Munc-18b Protein,Munc18 Syntaxin Binding Proteins,Munc18-1 Protein,Munc18-2 Protein,Munc18-3 Protein,Munc18a Protein,Munc18b Protein,Munc18c Protein,Sec1-Munc18 Protein Family,Syntaxin Binding Protein Munc18,Munc 18 Proteins,Sec1 Munc18 Protein Family
D029701 Saccharomyces cerevisiae Proteins Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes. Baker's Yeast Proteins,S cerevisiae Proteins

Related Publications

John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
March 1996, The Journal of biological chemistry,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
December 2012, Molecular biology of the cell,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
March 2003, Trends in biochemical sciences,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
February 1994, Proceedings of the National Academy of Sciences of the United States of America,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
November 1994, Neuron,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
December 2014, Current opinion in structural biology,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
July 2015, Nature structural & molecular biology,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
January 2003, Proceedings of the National Academy of Sciences of the United States of America,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
June 2006, The Journal of cell biology,
John Togneri, and Yi-Shan Cheng, and Mary Munson, and Frederick M Hughson, and Chavela M Carr
January 2012, PloS one,
Copied contents to your clipboard!