Endoplasmic Reticulum Export of GPI-Anchored Proteins.

Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus. The COPII machinery must adapt to the existing w...

Descripción completa

Detalles Bibliográficos
Autores: Lopez, Sergio, Rodriguez-Gallardo, Sofia, Sabido-Bozo, Susana, Muñiz, Manuel
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Instituto de Salud Carlos III (ISCIII)
Repositorio:Repisalud
Idioma:inglés
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/25251
Acceso en línea:https://hdl.handle.net/20.500.12105/25251
Access Level:acceso abierto
Palabra clave:COPII coat
GPI-anchored protein
Endoplasmic reticulum
p24 complex
Animals
COP-Coated Vesicles
Endoplasmic Reticulum
Golgi Apparatus
Humans
Membrane Proteins
Oligosaccharides
Protein Transport
id ES_a4e3cd1f99f575c313f8c3cecf029ef8
oai_identifier_str oai:repisalud.isciii.es:20.500.12105/25251
network_acronym_str ES
network_name_str España
repository_id_str
spelling Endoplasmic Reticulum Export of GPI-Anchored Proteins.Lopez, SergioRodriguez-Gallardo, SofiaSabido-Bozo, SusanaMuñiz, ManuelCOPII coatGPI-anchored proteinEndoplasmic reticulump24 complexAnimalsCOP-Coated VesiclesEndoplasmic ReticulumGolgi ApparatusHumansMembrane ProteinsOligosaccharidesProtein TransportProtein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus. The COPII machinery must adapt to the existing wide variety of different types of cargo proteins and to different cellular needs for cargo secretion. The study of the ER export of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs), a special glycolipid-linked class of cell surface proteins, is contributing to address these key issues. Due to their special biophysical properties, GPI-APs use a specialized COPII machinery to be exported from the ER and their processing and maturation has been recently shown to actively regulate COPII function. In this review, we discuss the regulatory mechanisms by which GPI-APs are assembled and selectively exported from the ER.20242024-10-2320192019-07-1720192019-07-17research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articlehttps://hdl.handle.net/20.500.12105/25251reponame:Repisaludinstname:Instituto de Salud Carlos III (ISCIII)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repisalud.isciii.es:20.500.12105/252512026-06-12T12:43:37Z
dc.title.none.fl_str_mv Endoplasmic Reticulum Export of GPI-Anchored Proteins.
title Endoplasmic Reticulum Export of GPI-Anchored Proteins.
spellingShingle Endoplasmic Reticulum Export of GPI-Anchored Proteins.
Lopez, Sergio
COPII coat
GPI-anchored protein
Endoplasmic reticulum
p24 complex
Animals
COP-Coated Vesicles
Endoplasmic Reticulum
Golgi Apparatus
Humans
Membrane Proteins
Oligosaccharides
Protein Transport
title_short Endoplasmic Reticulum Export of GPI-Anchored Proteins.
title_full Endoplasmic Reticulum Export of GPI-Anchored Proteins.
title_fullStr Endoplasmic Reticulum Export of GPI-Anchored Proteins.
title_full_unstemmed Endoplasmic Reticulum Export of GPI-Anchored Proteins.
title_sort Endoplasmic Reticulum Export of GPI-Anchored Proteins.
dc.creator.none.fl_str_mv Lopez, Sergio
Rodriguez-Gallardo, Sofia
Sabido-Bozo, Susana
Muñiz, Manuel
author Lopez, Sergio
author_facet Lopez, Sergio
Rodriguez-Gallardo, Sofia
Sabido-Bozo, Susana
Muñiz, Manuel
author_role author
author2 Rodriguez-Gallardo, Sofia
Sabido-Bozo, Susana
Muñiz, Manuel
author2_role author
author
author
dc.contributor.none.fl_str_mv
dc.subject.none.fl_str_mv COPII coat
GPI-anchored protein
Endoplasmic reticulum
p24 complex
Animals
COP-Coated Vesicles
Endoplasmic Reticulum
Golgi Apparatus
Humans
Membrane Proteins
Oligosaccharides
Protein Transport
topic COPII coat
GPI-anchored protein
Endoplasmic reticulum
p24 complex
Animals
COP-Coated Vesicles
Endoplasmic Reticulum
Golgi Apparatus
Humans
Membrane Proteins
Oligosaccharides
Protein Transport
description Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus. The COPII machinery must adapt to the existing wide variety of different types of cargo proteins and to different cellular needs for cargo secretion. The study of the ER export of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs), a special glycolipid-linked class of cell surface proteins, is contributing to address these key issues. Due to their special biophysical properties, GPI-APs use a specialized COPII machinery to be exported from the ER and their processing and maturation has been recently shown to actively regulate COPII function. In this review, we discuss the regulatory mechanisms by which GPI-APs are assembled and selectively exported from the ER.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-07-17
2019
2019-07-17
2024
2024-10-23
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.12105/25251
url https://hdl.handle.net/20.500.12105/25251
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:Repisalud
instname:Instituto de Salud Carlos III (ISCIII)
instname_str Instituto de Salud Carlos III (ISCIII)
reponame_str Repisalud
collection Repisalud
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869415551678283776
score 15.812429

Similares en LA Referencia