ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses

The conjugation of ATG8 (autophagy-related 8) proteins to the lipid phospha-tidylethanolamine (PE) is the result of the coordinated and highly regulated action of several ATG core proteins, including ATG4 proteases and the E1 (ATG7)- and E2 (ATG3)- activating enzymes. Although it has been stablished...

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Detalles Bibliográficos
Autores: Mallén Ponce, Manuel J., Pérez-Pérez, María Esther
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/181088
Acceso en línea:https://hdl.handle.net/11441/181088
https://doi.org/10.1080/27694127.2023.2300622
Access Level:acceso abierto
Palabra clave:ATG3 ATG8 lipidation Chlamydomonas ROS
Redox
Stress
Trx
Yeast
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repository_id_str
spelling ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stressesMallén Ponce, Manuel J.Pérez-Pérez, María EstherATG3 ATG8 lipidation Chlamydomonas ROSRedoxStressTrxYeastThe conjugation of ATG8 (autophagy-related 8) proteins to the lipid phospha-tidylethanolamine (PE) is the result of the coordinated and highly regulated action of several ATG core proteins, including ATG4 proteases and the E1 (ATG7)- and E2 (ATG3)- activating enzymes. Although it has been stablished that ROS signaling plays an important role in autophagy activation, the molecular mechanisms underlying the redox control of ATG proteins remain largely unclear. We have recently shown that ATG3 activity in Chlamydomonas rein- hardtii is subjected to reversible redox regulation to ensure ATG8 lipidation and autophagy progression under ROS-linked stress conditions.Taylor & Francis GroupBioquímica Vegetal y Biología MolecularMinisterio de Ciencia e Innovación2024info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/181088https://doi.org/10.1080/27694127.2023.2300622reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésAutophagy Reports, 3 (1), 2300622.PID2019- 110080GB-I00TED2021-130912B-I00https://www.tandfonline.com/doi/full/10.1080/27694127.2023.2300622info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1810882026-06-17T12:51:07Z
dc.title.none.fl_str_mv ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
title ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
spellingShingle ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
Mallén Ponce, Manuel J.
ATG3 ATG8 lipidation Chlamydomonas ROS
Redox
Stress
Trx
Yeast
title_short ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
title_full ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
title_fullStr ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
title_full_unstemmed ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
title_sort ATG3 is subjected to redox regulation to quarantee ATG8 lipidation under ROS-generating stresses
dc.creator.none.fl_str_mv Mallén Ponce, Manuel J.
Pérez-Pérez, María Esther
author Mallén Ponce, Manuel J.
author_facet Mallén Ponce, Manuel J.
Pérez-Pérez, María Esther
author_role author
author2 Pérez-Pérez, María Esther
author2_role author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Ministerio de Ciencia e Innovación
dc.subject.none.fl_str_mv ATG3 ATG8 lipidation Chlamydomonas ROS
Redox
Stress
Trx
Yeast
topic ATG3 ATG8 lipidation Chlamydomonas ROS
Redox
Stress
Trx
Yeast
description The conjugation of ATG8 (autophagy-related 8) proteins to the lipid phospha-tidylethanolamine (PE) is the result of the coordinated and highly regulated action of several ATG core proteins, including ATG4 proteases and the E1 (ATG7)- and E2 (ATG3)- activating enzymes. Although it has been stablished that ROS signaling plays an important role in autophagy activation, the molecular mechanisms underlying the redox control of ATG proteins remain largely unclear. We have recently shown that ATG3 activity in Chlamydomonas rein- hardtii is subjected to reversible redox regulation to ensure ATG8 lipidation and autophagy progression under ROS-linked stress conditions.
publishDate 2024
dc.date.none.fl_str_mv 2024
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/11441/181088
https://doi.org/10.1080/27694127.2023.2300622
url https://hdl.handle.net/11441/181088
https://doi.org/10.1080/27694127.2023.2300622
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Autophagy Reports, 3 (1), 2300622.
PID2019- 110080GB-I00
TED2021-130912B-I00
https://www.tandfonline.com/doi/full/10.1080/27694127.2023.2300622
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 Taylor & Francis Group
publisher.none.fl_str_mv Taylor & Francis Group
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 15,198674

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