The BioGRID Database Seperator
Search
Organism:

Cell Oct (1995); 83(1):111-9
Complexins: cytosolic proteins that regulate SNAP receptor function.
McMahon HT, Missler M, Li C, Sudhof TC
Howard Hughes Medical Institute, University of Texas Southwestern Medical School, Dallas 75235, USA.
Abstract: A family of proteins called complexins was discovered that compete with alpha-SNAP, but not synaptotagmin, for SNAP receptor binding. Complexins I and II are highly homologous hydrophilic proteins that are tightly conserved, with 100% identity among mouse, rat, and human complexin II. They are enriched in neurons where they colocalize with syntaxin and SNAP-25; in addition, complexin II is expressed ubiquitously at low levels. Complexins bind weakly to syntaxin alone and not at all to synaptobrevin and SNAP-25, but strongly to the SNAP receptor-core complex composed of these three molecules. They compete with alpha-SNAP for binding to the core complex but not with other interacting molecules, including synaptotagmin I, suggesting that the complexins regulate the sequential interactions of alpha-SNAP and synaptotagmins with the SNAP receptor during exocytosis.
[PUBMED: 7553862] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
terms and conditions - privacy policy - Osprey Network Visualization System
BioGRID: A General Repository for Interaction Datasets.
Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.