Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum

被引:9
|
作者
Lopez, Sergio
Maria Perez-Linero, Ana
Manzano-Lopez, Javier
Sabido-Bozo, Susana
Cortes-Gomez, Alejandro
Rodriguez-Gallardo, Sofia
Aguilera-Romero, Auxiliadora
Goder, Veit
Muniz, Manuel
机构
[1] Department of Cell Biology, University of Seville, Seville
[2] Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC, Universidad de Sevilla, Seville
[3] Department of Genetics, University of Seville, Seville
关键词
endoplasmic reticulum; cargo receptor; p24; complex; secretory cargo; bulk flow; GPI-ANCHORED PROTEINS; ER EXIT; TRANSPORT VESICLES; QUALITY-CONTROL; GOLGI; YEAST; SITES; ERV25P; EMP24P; RECEPTORS;
D O I
10.3390/cells9051295
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The cellular mechanisms that ensure the selectivity and fidelity of secretory cargo protein transport from the endoplasmic reticulum (ER) to the Golgi are still not well understood. The p24 protein complex acts as a specific cargo receptor for GPI-anchored proteins by facilitating their ER exit through a specialized export pathway in yeast. In parallel, the p24 complex can also exit the ER using the general pathway that exports the rest of secretory proteins with their respective cargo receptors. Here, we show biochemically that the p24 complex associates at the ER with other cargo receptors in a COPII-dependent manner, forming high-molecular weight multireceptor complexes. Furthermore, live cell imaging analysis reveals that the p24 complex is required to retain in the ER secretory cargos when their specific receptors are absent. This requirement does not involve neither the unfolded protein response nor the retrograde transport from the Golgi. Our results suggest that, in addition to its role as a cargo receptor in the specialized GPI-anchored protein pathway, the p24 complex also plays an independent role in secretory cargo selectivity during its exit through the general ER export pathway, preventing the non-selective bulk flow of native secretory cargos. This mechanism would ensure receptor-regulated cargo transport, providing an additional layer of regulation of secretory cargo selectivity during ER export.
引用
收藏
页数:17
相关论文
共 50 条
  • [21] The LPV Motif Is Essential for the Efficient Export of Secretory DMP1 From the Endoplasmic Reticulum
    Liang, Tian
    Meng, Tian
    Wang, Suzhen
    Qin, Chunlin
    Lu, Yongbo
    JOURNAL OF CELLULAR PHYSIOLOGY, 2016, 231 (07) : 1468 - 1475
  • [22] A di-acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum
    Nishimura, N
    Bannykh, S
    Slabough, S
    Matteson, J
    Altschuler, Y
    Hahn, K
    Balch, WE
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (22) : 15937 - 15946
  • [23] INVOLVEMENT OF A CYTOSOLIC PROTEIN COMPLEX IN PROTEIN EXPORT FROM THE ENDOPLASMIC-RETICULUM
    PETER, FJ
    PLUTNER, H
    BALCH, WE
    JOURNAL OF CELLULAR BIOCHEMISTRY, 1993, : 27 - 27
  • [24] Differential effects of a GTP-restricted mutant of Sar1p on segregation of cargo during export from the endoplasmic reticulum
    Stephens, DJ
    Pepperkok, R
    JOURNAL OF CELL SCIENCE, 2004, 117 (16) : 3635 - 3644
  • [25] Endoplasmic reticulum exit of a secretory glycoprotein in the absence of Sec24p family proteins in yeast
    Karhinen, L
    Bastos, RN
    Jokitalo, E
    Makarow, M
    TRAFFIC, 2005, 6 (07) : 562 - 574
  • [26] Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
    Wendeler, Markus W.
    Paccaud, Jean-Pierre
    Hauri, Hans-Peter
    EMBO REPORTS, 2007, 8 (03) : 258 - 264
  • [27] Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum
    Lu, Chung-Ling
    Ortmeier, Steven
    Brudvig, Jon
    Moretti, Tamara
    Cain, Jacob
    Boyadjiev, Simeon A.
    Weimer, Jill M.
    Kim, Jinoh
    TRAFFIC, 2022, 23 (01) : 81 - 93
  • [28] The Highly Conserved COPII Coat Complex Sorts Cargo from the Endoplasmic Reticulum and Targets It to the Golgi
    Lord, Christopher
    Ferro-Novick, Susan
    Miller, Elizabeth A.
    COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY, 2013, 5 (02):
  • [29] Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex
    Belden, WJ
    Barlowe, C
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (46) : 43040 - 43048
  • [30] Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane
    Pilon, M
    Römisch, K
    Quach, D
    Schekman, R
    MOLECULAR BIOLOGY OF THE CELL, 1998, 9 (12) : 3455 - 3473