The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling

被引:110
作者
Castillon, Guillaume A. [2 ]
Aguilera-Romero, Auxiliadora [1 ]
Manzano-Lopez, Javier [1 ]
Epstein, Sharon [2 ]
Kajiwara, Kentaro [3 ]
Funato, Kouichi [3 ]
Watanabe, Reika [2 ]
Riezman, Howard [2 ]
Muniz, Manuel [1 ]
机构
[1] Univ Seville, Dept Cell Biol, E-41012 Seville, Spain
[2] Univ Geneva, Dept Biochem Sci 2, CH-1211 Geneva 4, Switzerland
[3] Hiroshima Univ, Grad Sch Biosphere Sci, Dept Bioresource Sci & Technol, Higashihiroshima 7398528, Japan
基金
瑞士国家科学基金会;
关键词
COPII-COATED VESICLES; ENDOPLASMIC-RETICULUM; SACCHAROMYCES-CEREVISIAE; ER EXIT; TRANSMEMBRANE PROTEIN; INOSITOL DEACYLATION; PLASMA-MEMBRANE; FAMILY-MEMBERS; GOLGI-COMPLEX; EMP24P;
D O I
10.1091/mbc.E11-04-0294
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:2924 / 2936
页数:13
相关论文
共 50 条
[1]   The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus [J].
Aguilera-Romero, Auxiliadora ;
Kaminska, Joanna ;
Spang, Anne ;
Riezman, Howard ;
Muniz, Manuel .
JOURNAL OF CELL BIOLOGY, 2008, 180 (04) :713-720
[2]   Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast [J].
Bagnat, M ;
Keränen, S ;
Shevchenko, A ;
Shevchenko, A ;
Simons, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (07) :3254-3259
[3]   Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex [J].
Belden, WJ ;
Barlowe, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (46) :43040-43048
[4]   Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport [J].
Belden, WJ ;
Barlowe, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (43) :26939-26946
[5]   Selective export of human GPI-anchored proteins from the endoplasmic reticulum [J].
Bonnon, Carine ;
Wendeler, Markus W. ;
Paccaud, Jean-Pierre ;
Hauri, Hans-Peter .
JOURNAL OF CELL SCIENCE, 2010, 123 (10) :1705-1715
[6]   Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors [J].
Bremser, M ;
Nickel, W ;
Schweikert, M ;
Ravazzola, M ;
Amherdt, M ;
Hughes, CA ;
Söllner, TH ;
Rothman, JE ;
Wieland, FT .
CELL, 1999, 96 (04) :495-506
[7]  
Caro LHP, 1997, YEAST, V13, P1477, DOI 10.1002/(SICI)1097-0061(199712)13:15<1477::AID-YEA184>3.0.CO
[8]  
2-L
[9]   Concentration of GPI-Anchored Proteins upon ER Exit in Yeast [J].
Castillon, Guillaume A. ;
Watanabe, Reika ;
Taylor, Marcia ;
Schwabe, Tatjana M. E. ;
Riezman, Howard .
TRAFFIC, 2009, 10 (02) :186-200
[10]   A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response [J].
Cox, JS ;
Walter, P .
CELL, 1996, 87 (03) :391-404