Muñiz Manuel, Riezman Howard
Departamento de Biología Celular, Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, Seville, Spain Universidad de Sevilla and Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, Seville, Spain
National Centre of Competence in Research (NCCR) Chemical Biology, Department of Biochemistry, University of Geneva, Geneva, Switzerland.
J Lipid Res. 2016 Mar;57(3):352-60. doi: 10.1194/jlr.R062760. Epub 2015 Oct 8.
In eukaryotes, many cell surface proteins are attached to the plasma membrane via a glycolipid glycosylphosphatidylinositol (GPI) anchor. GPI-anchored proteins (GPI-APs) receive the GPI anchor as a conserved posttranslational modification in the lumen of the endoplasmic reticulum (ER). After anchor attachment, the GPI anchor is structurally remodeled to function as a transport signal that actively triggers the delivery of GPI-APs from the ER to the plasma membrane, via the Golgi apparatus. The structure and composition of the GPI anchor confer a special mode of interaction with membranes of GPI-APs within the lumen of secretory organelles that lead them to be differentially trafficked from other secretory membrane proteins. In this review, we examine the mechanisms by which GPI-APs are selectively transported through the secretory pathway, with special focus on the recent progress made in their actively regulated export from the ER and the trans-Golgi network.
在真核生物中，许多细胞表面蛋白通过糖脂糖基磷脂酰肌醇（GPI）锚定连接到质膜上。GPI锚定蛋白（GPI-APs）在内质网（ER）腔中作为一种保守的翻译后修饰接受GPI锚定。锚定连接后，GPI锚定在结构上被重塑，作为一种转运信号，通过高尔基体主动触发GPI-APs从内质网到质膜的转运。GPI锚定的结构和组成赋予了与分泌细胞器腔内GPI-APs膜的一种特殊相互作用模式，导致它们与其他分泌膜蛋白的转运方式不同。在这篇综述中，我们研究了GPI-APs通过分泌途径选择性转运的机制，特别关注它们从内质网和反式高尔基体网络主动调控输出方面的最新进展。
