The ULK1-FBXW5-SEC23B nexus controls autophagy

Autores
Jeong, Yeon-Tae; Simoneschi, Daniele; Keegan, Sarah; Melville, David; Adler, Natalia Sol; Saraf, Anita; Florens, Laurence; Washburn, Michael P.; Cavasotto, Claudio Norberto; Fenyö, David; Sanchez Cuervo, Ana Maria; Rossi, Mario; Pagano, Michele
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In response to nutrient deprivation, the cell mobilizes an extensive amount of membrane to form and grow the autophagosome, allowing the progression of autophagy. By providing membranes and stimulating LC3 lipidation, COPII (Coat Protein Complex II) promotes autophagosome biogenesis. Here, we show that the F-box protein FBXW5 targets SEC23B, a component of COPII, for proteasomal degradation and that this event limits the autophagic flux in the presence of nutrients. In response to starvation, ULK1 phosphorylates SEC23B on Serine 186, preventing the interaction of SEC23B with FBXW5 and, therefore, inhibiting SEC23B degradation. Phosphorylated and stabilized SEC23B associates with SEC24A and SEC24B, but not SEC24C and SEC24D, and they re-localize to the ER-Golgi intermediate compartment, promoting autophagic flux. We propose that, in the presence of nutrients, FBXW5 limits COPII-mediated autophagosome biogenesis. Inhibition of this event by ULK1 ensures efficient execution of the autophagic cascade in response to nutrient starvation.
Fil: Jeong, Yeon-Tae. Nyu School Of Medicine;
Fil: Simoneschi, Daniele. Nyu School Of Medicine;
Fil: Keegan, Sarah. Nyu School Of Medicine;
Fil: Melville, David. University of California at Berkeley; Estados Unidos
Fil: Adler, Natalia Sol. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Saraf, Anita. Universidad Austral; Argentina
Fil: Florens, Laurence. Stowers Institute For Medical Research;
Fil: Washburn, Michael P.. Stowers Institute For Medical Research;
Fil: Cavasotto, Claudio Norberto. University Of Kansas Medical Center;
Fil: Fenyö, David. Stowers Institute For Medical Research;
Fil: Cuervo, Ana-Maria. Universidad Austral; Argentina
Fil: Rossi, Mario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pagano, Michele. Nyu School Of Medicine;
Materia
CRLS
SCF
ULK1
AUTOPHAGY
CANCER
CELL
CELL BIOLOGY
HUMAN
UBIQUITIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/93851
Acceder
id CONICETDig_2bb1f65f7b16a3339b851f8bd31a1d7c
oai_identifier_str oai:ri.conicet.gov.ar:11336/93851
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The ULK1-FBXW5-SEC23B nexus controls autophagyJeong, Yeon-TaeSimoneschi, DanieleKeegan, SarahMelville, DavidAdler, Natalia SolSaraf, AnitaFlorens, LaurenceWashburn, Michael P.Cavasotto, Claudio NorbertoFenyö, DavidSanchez Cuervo, Ana MariaRossi, MarioPagano, MicheleCRLSSCFULK1AUTOPHAGYCANCERCELLCELL BIOLOGYHUMANUBIQUITINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In response to nutrient deprivation, the cell mobilizes an extensive amount of membrane to form and grow the autophagosome, allowing the progression of autophagy. By providing membranes and stimulating LC3 lipidation, COPII (Coat Protein Complex II) promotes autophagosome biogenesis. Here, we show that the F-box protein FBXW5 targets SEC23B, a component of COPII, for proteasomal degradation and that this event limits the autophagic flux in the presence of nutrients. In response to starvation, ULK1 phosphorylates SEC23B on Serine 186, preventing the interaction of SEC23B with FBXW5 and, therefore, inhibiting SEC23B degradation. Phosphorylated and stabilized SEC23B associates with SEC24A and SEC24B, but not SEC24C and SEC24D, and they re-localize to the ER-Golgi intermediate compartment, promoting autophagic flux. We propose that, in the presence of nutrients, FBXW5 limits COPII-mediated autophagosome biogenesis. Inhibition of this event by ULK1 ensures efficient execution of the autophagic cascade in response to nutrient starvation.Fil: Jeong, Yeon-Tae. Nyu School Of Medicine;Fil: Simoneschi, Daniele. Nyu School Of Medicine;Fil: Keegan, Sarah. Nyu School Of Medicine;Fil: Melville, David. University of California at Berkeley; Estados UnidosFil: Adler, Natalia Sol. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Saraf, Anita. Universidad Austral; ArgentinaFil: Florens, Laurence. Stowers Institute For Medical Research;Fil: Washburn, Michael P.. Stowers Institute For Medical Research;Fil: Cavasotto, Claudio Norberto. University Of Kansas Medical Center;Fil: Fenyö, David. Stowers Institute For Medical Research;Fil: Cuervo, Ana-Maria. Universidad Austral; ArgentinaFil: Rossi, Mario. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Pagano, Michele. Nyu School Of Medicine;eLife Sciences Publications2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/93851Jeong, Yeon-Tae; Simoneschi, Daniele; Keegan, Sarah; Melville, David; Adler, Natalia Sol; et al.; The ULK1-FBXW5-SEC23B nexus controls autophagy; eLife Sciences Publications; eLife; 7; 12-2018; 42253-422532050-084XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/42253info:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.42253info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:25:56Zoai:ri.conicet.gov.ar:11336/93851instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:25:56.439CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The ULK1-FBXW5-SEC23B nexus controls autophagy
title The ULK1-FBXW5-SEC23B nexus controls autophagy
spellingShingle The ULK1-FBXW5-SEC23B nexus controls autophagy
Jeong, Yeon-Tae
CRLS
SCF
ULK1
AUTOPHAGY
CANCER
CELL
CELL BIOLOGY
HUMAN
UBIQUITIN
title_short The ULK1-FBXW5-SEC23B nexus controls autophagy
title_full The ULK1-FBXW5-SEC23B nexus controls autophagy
title_fullStr The ULK1-FBXW5-SEC23B nexus controls autophagy
title_full_unstemmed The ULK1-FBXW5-SEC23B nexus controls autophagy
title_sort The ULK1-FBXW5-SEC23B nexus controls autophagy
dc.creator.none.fl_str_mv Jeong, Yeon-Tae
Simoneschi, Daniele
Keegan, Sarah
Melville, David
Adler, Natalia Sol
Saraf, Anita
Florens, Laurence
Washburn, Michael P.
Cavasotto, Claudio Norberto
Fenyö, David
Sanchez Cuervo, Ana Maria
Rossi, Mario
Pagano, Michele
author Jeong, Yeon-Tae
author_facet Jeong, Yeon-Tae
Simoneschi, Daniele
Keegan, Sarah
Melville, David
Adler, Natalia Sol
Saraf, Anita
Florens, Laurence
Washburn, Michael P.
Cavasotto, Claudio Norberto
Fenyö, David
Sanchez Cuervo, Ana Maria
Rossi, Mario
Pagano, Michele
author_role author
author2 Simoneschi, Daniele
Keegan, Sarah
Melville, David
Adler, Natalia Sol
Saraf, Anita
Florens, Laurence
Washburn, Michael P.
Cavasotto, Claudio Norberto
Fenyö, David
Sanchez Cuervo, Ana Maria
Rossi, Mario
Pagano, Michele
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CRLS
SCF
ULK1
AUTOPHAGY
CANCER
CELL
CELL BIOLOGY
HUMAN
UBIQUITIN
topic CRLS
SCF
ULK1
AUTOPHAGY
CANCER
CELL
CELL BIOLOGY
HUMAN
UBIQUITIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In response to nutrient deprivation, the cell mobilizes an extensive amount of membrane to form and grow the autophagosome, allowing the progression of autophagy. By providing membranes and stimulating LC3 lipidation, COPII (Coat Protein Complex II) promotes autophagosome biogenesis. Here, we show that the F-box protein FBXW5 targets SEC23B, a component of COPII, for proteasomal degradation and that this event limits the autophagic flux in the presence of nutrients. In response to starvation, ULK1 phosphorylates SEC23B on Serine 186, preventing the interaction of SEC23B with FBXW5 and, therefore, inhibiting SEC23B degradation. Phosphorylated and stabilized SEC23B associates with SEC24A and SEC24B, but not SEC24C and SEC24D, and they re-localize to the ER-Golgi intermediate compartment, promoting autophagic flux. We propose that, in the presence of nutrients, FBXW5 limits COPII-mediated autophagosome biogenesis. Inhibition of this event by ULK1 ensures efficient execution of the autophagic cascade in response to nutrient starvation.
Fil: Jeong, Yeon-Tae. Nyu School Of Medicine;
Fil: Simoneschi, Daniele. Nyu School Of Medicine;
Fil: Keegan, Sarah. Nyu School Of Medicine;
Fil: Melville, David. University of California at Berkeley; Estados Unidos
Fil: Adler, Natalia Sol. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Saraf, Anita. Universidad Austral; Argentina
Fil: Florens, Laurence. Stowers Institute For Medical Research;
Fil: Washburn, Michael P.. Stowers Institute For Medical Research;
Fil: Cavasotto, Claudio Norberto. University Of Kansas Medical Center;
Fil: Fenyö, David. Stowers Institute For Medical Research;
Fil: Cuervo, Ana-Maria. Universidad Austral; Argentina
Fil: Rossi, Mario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pagano, Michele. Nyu School Of Medicine;
description In response to nutrient deprivation, the cell mobilizes an extensive amount of membrane to form and grow the autophagosome, allowing the progression of autophagy. By providing membranes and stimulating LC3 lipidation, COPII (Coat Protein Complex II) promotes autophagosome biogenesis. Here, we show that the F-box protein FBXW5 targets SEC23B, a component of COPII, for proteasomal degradation and that this event limits the autophagic flux in the presence of nutrients. In response to starvation, ULK1 phosphorylates SEC23B on Serine 186, preventing the interaction of SEC23B with FBXW5 and, therefore, inhibiting SEC23B degradation. Phosphorylated and stabilized SEC23B associates with SEC24A and SEC24B, but not SEC24C and SEC24D, and they re-localize to the ER-Golgi intermediate compartment, promoting autophagic flux. We propose that, in the presence of nutrients, FBXW5 limits COPII-mediated autophagosome biogenesis. Inhibition of this event by ULK1 ensures efficient execution of the autophagic cascade in response to nutrient starvation.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/93851
Jeong, Yeon-Tae; Simoneschi, Daniele; Keegan, Sarah; Melville, David; Adler, Natalia Sol; et al.; The ULK1-FBXW5-SEC23B nexus controls autophagy; eLife Sciences Publications; eLife; 7; 12-2018; 42253-42253
2050-084X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/93851
identifier_str_mv Jeong, Yeon-Tae; Simoneschi, Daniele; Keegan, Sarah; Melville, David; Adler, Natalia Sol; et al.; The ULK1-FBXW5-SEC23B nexus controls autophagy; eLife Sciences Publications; eLife; 7; 12-2018; 42253-42253
2050-084X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/42253
info:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.42253
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv eLife Sciences Publications
publisher.none.fl_str_mv eLife Sciences Publications
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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