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外排性SNARE蛋白的质膜靶向作用。

Plasma membrane targeting of exocytic SNARE proteins.

作者信息

Salaün Christine, James Declan J, Greaves Jennifer, Chamberlain Luke H

机构信息

Henry Wellcome Laboratory of Cell Biology, Division of Biochemistry & Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, United Kingdom.

出版信息

Biochim Biophys Acta. 2004 Aug 23;1693(2):81-9. doi: 10.1016/j.bbamcr.2004.05.008.

Abstract

SNARE proteins play a central role in the process of intracellular membrane fusion. Indeed, the interaction of SNAREs present on two opposing membranes is generally believed to provide the driving force to initiate membrane fusion. Eukaryotic cells express a large number of SNARE isoforms, and the function of individual SNAREs is required for specific intracellular fusion events. Exocytosis, the fusion of secretory vesicles with the plasma membrane, employs the proteins syntaxin and SNAP-25 as plasma membrane SNAREs. As a result, exocytosis is dependent upon the targeting of these proteins to the plasma membrane; however, the mechanisms that underlie trafficking of exocytic syntaxin and SNAP-25 proteins to the cell surface are poorly understood. The intracellular trafficking itinerary of these proteins is particularly intriguing as syntaxins are tail-anchored (or Type IV) membrane proteins, whereas SNAP-25 is anchored to membranes via a central palmitoylated domain-there is no common consensus for the trafficking of such proteins within the cell. In this review, we discuss the plasma membrane targeting of these essential exocytic SNARE proteins.

摘要

SNARE蛋白在细胞内膜融合过程中发挥着核心作用。实际上,通常认为存在于两个相对膜上的SNARE之间的相互作用为启动膜融合提供了驱动力。真核细胞表达大量的SNARE异构体,特定的细胞内融合事件需要单个SNARE的功能。胞吐作用,即分泌小泡与质膜的融合,利用 syntaxin和SNAP-25蛋白作为质膜SNARE。因此,胞吐作用依赖于这些蛋白靶向到质膜;然而,将胞吐性syntaxin和SNAP-25蛋白运输到细胞表面的潜在机制仍知之甚少。这些蛋白的细胞内运输路径特别引人关注,因为syntaxin是尾锚定(或IV型)膜蛋白,而SNAP-25是通过中央棕榈酰化结构域锚定在膜上的——对于此类蛋白在细胞内的运输没有共同的共识。在这篇综述中,我们讨论了这些必需的胞吐SNARE蛋白的质膜靶向。

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