首页 | 本学科首页   官方微博 | 高级检索  
   检索      


The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling
Authors:Castillon Guillaume A  Aguilera-Romero Auxiliadora  Manzano-Lopez Javier  Epstein Sharon  Kajiwara Kentaro  Funato Kouichi  Watanabe Reika  Riezman Howard  Muñiz Manuel
Institution:Department of Biochemistry, Sciences II, University of Geneva, CH-1211 Geneva 4, Switzerland.
Abstract:Glycosylphosphatidylinositol (GPI)-anchored proteins are secretory proteins that are attached to the cell surface of eukaryotic cells by a glycolipid moiety. Once GPI anchoring has occurred in the lumen of the endoplasmic reticulum (ER), the structure of the lipid part on the GPI anchor undergoes a remodeling process prior to ER exit. In this study, we provide evidence suggesting that the yeast p24 complex, through binding specifically to GPI-anchored proteins in an anchor-dependent manner, plays a dual role in their selective trafficking. First, the p24 complex promotes efficient ER exit of remodeled GPI-anchored proteins after concentration by connecting them with the COPII coat and thus facilitates their incorporation into vesicles. Second, it retrieves escaped, unremodeled GPI-anchored proteins from the Golgi to the ER in COPI vesicles. Therefore the p24 complex, by sensing the status of the GPI anchor, regulates GPI-anchored protein intracellular transport and coordinates this with correct anchor remodeling.
Keywords:
本文献已被 PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号