Steegmaier M, Yang B, Yoo J S, Huang B, Shen M, Yu S, Luo Y, Scheller R H
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305-5345, USA.
J Biol Chem. 1998 Dec 18;273(51):34171-9. doi: 10.1074/jbc.273.51.34171.
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.
细胞内膜运输被认为部分受可溶性N - 乙基马来酰亚胺敏感因子附着蛋白受体（SNAREs）调控，这些蛋白质存在于囊泡膜和靶膜上，通过形成复合物来发挥作用。所有已知的SNARE介导的融合事件都涉及 syntaxin和囊泡相关膜蛋白家族的成员。哺乳动物膜区室的多样性预示着存在大量不同的syntaxin和囊泡相关膜蛋白基因。为了进一步研究SNAREs的种类及其在膜运输中的作用，我们鉴定了syntaxin和SNAP - 25（25 kDa突触体相关蛋白）亚家族的三个新成员。这些蛋白质广泛表达，表明它们在囊泡运输中具有普遍作用，并定位于不同的膜区室。Syntaxin 8与内质网标记物共定位。Syntaxin 17是syntaxin家族的一个不同成员，部分与内质网标记物重叠，而SNAP - 29广泛定位于多种膜上。SNAP - 29不包含其他SNAREs预测的膜锚定结构。体外研究表明，SNAP - 29能够与多种syntaxin结合。
