The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus

被引:53
作者
Aguilera-Romero, Auxiliadora [1 ]
Kaminska, Joanna [2 ]
Spang, Anne [3 ]
Riezman, Howard [4 ]
Muniz, Manuel [1 ]
机构
[1] Univ Seville, Dept Cell Biol, E-41012 Seville, Spain
[2] Inst Biochem & Biophys PAS, PL-02106 Warsaw, Poland
[3] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland
[4] Univ Geneva, Dept Biochem, CH-1211 Geneva, Switzerland
关键词
D O I
10.1083/jcb.200710025
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The p24 family members are transmembrane proteins assembled into heteromeric complexes that continuously cycle between the ER and the Golgi apparatus. These cargo proteins were assumed to play a structural role in COPI budding because of their major presence in mammalian COPI vesicles. However, this putative function has not been proved conclusively so far. Furthermore, deletion of all eight yeast p24 family members does not produce severe transport phenotypes, suggesting that the p24 complex is not essential for CON function. In this paper we provide direct evidence that the yeast p24 complex plays an active role in retrograde transport from Golgi to ER by facilitating the formation of COPI-coated vesicles. Therefore, our results demonstrate that p24 proteins are important for vesicle formation instead of simply being a passive traveler, supporting the model in which cargo together with a small GTPase of the ARF superfamily and coat subunits act as primer for vesicle formation.
引用
收藏
页码:713 / 720
页数:8
相关论文
共 46 条
[1]   Deletion of yeast p24 genes activates the unfolded protein response [J].
Belden, WJ ;
Barlowe, C .
MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (04) :957-969
[2]   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
[3]   Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins [J].
Bethune, Julien ;
Kol, Matthijs ;
Hoffmann, Julia ;
Reckmann, Inge ;
Bruegger, Britta ;
Wieland, Felix .
MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (21) :8011-8021
[4]   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
[5]   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
[6]   The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval [J].
Dogic, D ;
de Chassey, B ;
Pick, E ;
Cassey, D ;
Lefkir, Y ;
Hennecke, S ;
Cosson, P ;
Letourneur, F .
EUROPEAN JOURNAL OF CELL BIOLOGY, 1999, 78 (05) :305-310
[7]  
DUDEN R, 1994, J BIOL CHEM, V269, P24486
[8]   Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations [J].
ElrodErickson, MJ ;
Kaiser, CA .
MOLECULAR BIOLOGY OF THE CELL, 1996, 7 (07) :1043-1058
[9]   The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics [J].
Emery, G ;
Parton, RG ;
Rojo, M ;
Gruenberg, J .
JOURNAL OF CELL SCIENCE, 2003, 116 (23) :4821-4832
[10]  
ESMON PC, 1987, J BIOL CHEM, V262, P4387