title: Three novel proteins of the syntaxin/SNAP-25 family.
abstract: 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.
authors.affiliation: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305-5345, USA.
authors.forename: M
authors.initials: M
authors.lastname: Steegmaier
authors.forename: B
authors.initials: B
authors.lastname: Yang
authors.forename: J S
authors.initials: JS
authors.lastname: Yoo
authors.forename: B
authors.initials: B
authors.lastname: Huang
authors.forename: M
authors.initials: M
authors.lastname: Shen
authors.forename: S
authors.initials: S
authors.lastname: Yu
authors.forename: Y
authors.initials: Y
authors.lastname: Luo
authors.forename: R H
authors.initials: RH
authors.lastname: Scheller
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D019556:COS Cells; D002460:Cell Line; D016208:Databases, Factual; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005033:Ethylmaleimide / Q000494:pharmacology; D019143:Evolution, Molecular; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D005810:Multigene Family; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D050765:Qa-SNARE Proteins; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D050825:Synaptosomal-Associated Protein 25; D014162:Transfection
chemical_list: D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; D011994:Recombinant Proteins; C494208:SNAP25 protein, human; C494210:Snap25 protein, rat; D050825:Synaptosomal-Associated Protein 25; D005033:Ethylmaleimide