Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases

Protein ubiquitylation acts as a complex cell signaling mechanism since the formation of different mono- and polyubiquitin chains determines the substrate's fate in the cell. E3 ligases define the specificity of this reaction by catalyzing the attachment of ubiquitin to the substrate protein. T...

Descripción completa

Detalles Bibliográficos
Autores: Sala Gastón, Joan, Costa-Sastre, Laura, Pedrazza, Leonardo, Martinez-Martinez, Arturo, Ventura Pujol, Francesc, Rosa López, José Luis
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/197266
Acceso en línea:https://hdl.handle.net/2445/197266
Access Level:acceso abierto
Palabra clave:Ubiqüitina
Tumors
Interacció cel·lular
Proteïnes quinases
Ubiquitin
Cell interaction
Protein kinases
id ES_274fc0c2bbd74be5f3972e7be1440b1e
oai_identifier_str oai:recercat.cat:2445/197266
network_acronym_str ES
network_name_str España
repository_id_str
spelling Regulation of MAPK signaling pathways by the large HERC ubiquitin ligasesSala Gastón, JoanCosta-Sastre, LauraPedrazza, LeonardoMartinez-Martinez, ArturoVentura Pujol, FrancescRosa López, José LuisUbiqüitinaTumorsInteracció cel·lularProteïnes quinasesUbiquitinTumorsCell interactionProtein kinasesProtein ubiquitylation acts as a complex cell signaling mechanism since the formation of different mono- and polyubiquitin chains determines the substrate's fate in the cell. E3 ligases define the specificity of this reaction by catalyzing the attachment of ubiquitin to the substrate protein. Thus, they represent an important regulatory component of this process. Large HERC ubiquitin ligases belong to the HECT E3 protein family and comprise HERC1 and HERC2 proteins. The physiological relevance of the Large HERCs is illustrated by their involvement in different pathologies, with a notable implication in cancer and neurological diseases. Understanding how cell signaling is altered in these different pathologies is important for uncovering novel therapeutic targets. To this end, this review summarizes the recent advances in how the Large HERCs regulate the MAPK signaling pathways. In addition, we emphasize the potential therapeutic strategies that could be followed to ameliorate the alterations in MAPK signaling caused by Large HERC deficiencies, focusing on the use of specific inhibitors and proteolysis-targeting chimeras.MDPI2023202320232023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion16 p.application/pdfhttps://hdl.handle.net/2445/197266Articles publicats en revistes (Ciències Fisiològiques)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.3390/ijms24054906International Journal of Molecular Sciences, 2023, vol. 24, num. 5https://doi.org/10.3390/ijms24054906cc-by (c) Sala Gaston, Joan et al., 2023https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1972662026-05-29T05:05:01Z
dc.title.none.fl_str_mv Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
title Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
spellingShingle Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
Sala Gastón, Joan
Ubiqüitina
Tumors
Interacció cel·lular
Proteïnes quinases
Ubiquitin
Tumors
Cell interaction
Protein kinases
title_short Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
title_full Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
title_fullStr Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
title_full_unstemmed Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
title_sort Regulation of MAPK signaling pathways by the large HERC ubiquitin ligases
dc.creator.none.fl_str_mv Sala Gastón, Joan
Costa-Sastre, Laura
Pedrazza, Leonardo
Martinez-Martinez, Arturo
Ventura Pujol, Francesc
Rosa López, José Luis
author Sala Gastón, Joan
author_facet Sala Gastón, Joan
Costa-Sastre, Laura
Pedrazza, Leonardo
Martinez-Martinez, Arturo
Ventura Pujol, Francesc
Rosa López, José Luis
author_role author
author2 Costa-Sastre, Laura
Pedrazza, Leonardo
Martinez-Martinez, Arturo
Ventura Pujol, Francesc
Rosa López, José Luis
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ubiqüitina
Tumors
Interacció cel·lular
Proteïnes quinases
Ubiquitin
Tumors
Cell interaction
Protein kinases
topic Ubiqüitina
Tumors
Interacció cel·lular
Proteïnes quinases
Ubiquitin
Tumors
Cell interaction
Protein kinases
description Protein ubiquitylation acts as a complex cell signaling mechanism since the formation of different mono- and polyubiquitin chains determines the substrate's fate in the cell. E3 ligases define the specificity of this reaction by catalyzing the attachment of ubiquitin to the substrate protein. Thus, they represent an important regulatory component of this process. Large HERC ubiquitin ligases belong to the HECT E3 protein family and comprise HERC1 and HERC2 proteins. The physiological relevance of the Large HERCs is illustrated by their involvement in different pathologies, with a notable implication in cancer and neurological diseases. Understanding how cell signaling is altered in these different pathologies is important for uncovering novel therapeutic targets. To this end, this review summarizes the recent advances in how the Large HERCs regulate the MAPK signaling pathways. In addition, we emphasize the potential therapeutic strategies that could be followed to ameliorate the alterations in MAPK signaling caused by Large HERC deficiencies, focusing on the use of specific inhibitors and proteolysis-targeting chimeras.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
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/2445/197266
url https://hdl.handle.net/2445/197266
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/ijms24054906
International Journal of Molecular Sciences, 2023, vol. 24, num. 5
https://doi.org/10.3390/ijms24054906
dc.rights.none.fl_str_mv cc-by (c) Sala Gaston, Joan et al., 2023
https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Sala Gaston, Joan et al., 2023
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 16 p.
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Ciències Fisiològiques)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869404878775779328
score 15,811543

Similares en LA Referencia