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

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 thro...

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Detalhes bibliográficos
Autores: López Martín, Sergio, Pérez Linero, Ana María, Manzano López, Javier, Sabido Bozo, Susana, Cortés Gómez, Alejandro, Rodríguez Gallardo, Sofía, Aguilera Romero, María Auxiliadora, Goder, Veit, Muñiz Guinea, Manuel
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Recursos:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/98123
Acesso em linha:https://hdl.handle.net/11441/98123
https://doi.org/10.3390/cells9051295
Access Level:acceso abierto
Palavra-chave:Bulk flow
Cargo receptor
Endoplasmic reticulum
p24 complex
Secretory cargo
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spelling Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic ReticulumLópez Martín, SergioPérez Linero, Ana MaríaManzano López, JavierSabido Bozo, SusanaCortés Gómez, AlejandroRodríguez Gallardo, SofíaAguilera Romero, María AuxiliadoraGoder, VeitMuñiz Guinea, ManuelBulk flowCargo receptorEndoplasmic reticulump24 complexSecretory cargoThe 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.Ministerio de Economía y Competitividad BFU2017-89700-P, BFU2016-78265-PMultidisciplinary Digital Publishing Institute (MDPI)Biología CelularGenética2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/98123https://doi.org/10.3390/cells9051295reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésCells, 9 (5), 1295.BFU2017-89700-PBFU2016-78265-Phttps://doi.org/10.3390/cells9051295info:eu-repo/semantics/openAccessoai:idus.us.es:11441/981232026-06-17T12:51:07Z
dc.title.none.fl_str_mv Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
title Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
spellingShingle Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
López Martín, Sergio
Bulk flow
Cargo receptor
Endoplasmic reticulum
p24 complex
Secretory cargo
title_short Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
title_full Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
title_fullStr Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
title_full_unstemmed Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
title_sort Dual Independent Roles of the p24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum
dc.creator.none.fl_str_mv López Martín, Sergio
Pérez Linero, Ana María
Manzano López, Javier
Sabido Bozo, Susana
Cortés Gómez, Alejandro
Rodríguez Gallardo, Sofía
Aguilera Romero, María Auxiliadora
Goder, Veit
Muñiz Guinea, Manuel
author López Martín, Sergio
author_facet López Martín, Sergio
Pérez Linero, Ana María
Manzano López, Javier
Sabido Bozo, Susana
Cortés Gómez, Alejandro
Rodríguez Gallardo, Sofía
Aguilera Romero, María Auxiliadora
Goder, Veit
Muñiz Guinea, Manuel
author_role author
author2 Pérez Linero, Ana María
Manzano López, Javier
Sabido Bozo, Susana
Cortés Gómez, Alejandro
Rodríguez Gallardo, Sofía
Aguilera Romero, María Auxiliadora
Goder, Veit
Muñiz Guinea, Manuel
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Biología Celular
Genética
dc.subject.none.fl_str_mv Bulk flow
Cargo receptor
Endoplasmic reticulum
p24 complex
Secretory cargo
topic Bulk flow
Cargo receptor
Endoplasmic reticulum
p24 complex
Secretory cargo
description 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.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/98123
https://doi.org/10.3390/cells9051295
url https://hdl.handle.net/11441/98123
https://doi.org/10.3390/cells9051295
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Cells, 9 (5), 1295.
BFU2017-89700-P
BFU2016-78265-P
https://doi.org/10.3390/cells9051295
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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