GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com


Jump to: navigation, search


You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki

See Help for Help on this wiki. See the documentation for how to use the table editor


Steegmaier, M, Yang, B, Yoo, JS, Huang, B, Shen, M, Yu, S, Luo, Y and Scheller, RH (1998) Three novel proteins of the syntaxin/SNAP-25 family. J. Biol. Chem. 273:34171-9


Intracellular membrane traffic is thought to be regulated in part by soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (SNAREs) through the formation of complexes between these proteins present on vesicle and target membranes. All known SNARE-mediated fusion events involve members of the syntaxin and vesicle-associated membrane protein families. The diversity of mammalian membrane compartments predicts the existence of a large number of different syntaxin and vesicle-associated membrane protein genes. To further investigate the spectrum of SNAREs and their roles in membrane trafficking we characterized three novel members of the syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) subfamilies. The proteins are broadly expressed, suggesting a general role in vesicle trafficking, and localize to distinct membrane compartments. Syntaxin 8 co-localizes with markers of the endoplasmic reticulum. Syntaxin 17, a divergent member of the syntaxin family, partially overlaps with endoplasmic reticulum markers, and SNAP-29 is broadly localized on multiple membranes. SNAP-29 does not contain a predicted membrane anchor characteristic of other SNAREs. In vitro studies established that SNAP-29 is capable of binding to a broad range of syntaxins.




Amino Acid Sequence; Animals; Blotting, Northern; COS Cells; Cell Line; Databases, Factual; Endoplasmic Reticulum/metabolism; Ethylmaleimide/pharmacology; Evolution, Molecular; Humans; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/isolation & purification; Molecular Sequence Data; Multigene Family; Nerve Tissue Proteins/chemistry; Nerve Tissue Proteins/genetics; Nerve Tissue Proteins/metabolism; Phylogeny; Qa-SNARE Proteins; Rats; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Synaptosomal-Associated Protein 25; Transfection