A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B

Upon autophagy induction, LC3 is cleaved by the protease ATG4 and conjugated to the autophagosomal membrane; however, its removal is mediated by the same protease. Here the authors show that ULK1-mediated phosphorylation and PP2A-mediated dephosphorylation of ATG4 regulates its cellular activity to...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: N. Pengo, A. Agrotis, K. Prak, J. Jones, R. Ketteler
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
Materias:
Q
Acceso en línea:https://doaj.org/article/be9d8c9445e94d1a89cc7a77d68e8daf
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:be9d8c9445e94d1a89cc7a77d68e8daf
record_format dspace
spelling oai:doaj.org-article:be9d8c9445e94d1a89cc7a77d68e8daf2021-12-02T13:57:54ZA reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B10.1038/s41467-017-00303-22041-1723https://doaj.org/article/be9d8c9445e94d1a89cc7a77d68e8daf2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00303-2https://doaj.org/toc/2041-1723Upon autophagy induction, LC3 is cleaved by the protease ATG4 and conjugated to the autophagosomal membrane; however, its removal is mediated by the same protease. Here the authors show that ULK1-mediated phosphorylation and PP2A-mediated dephosphorylation of ATG4 regulates its cellular activity to control LC3 processing.N. PengoA. AgrotisK. PrakJ. JonesR. KettelerNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
N. Pengo
A. Agrotis
K. Prak
J. Jones
R. Ketteler
A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
description Upon autophagy induction, LC3 is cleaved by the protease ATG4 and conjugated to the autophagosomal membrane; however, its removal is mediated by the same protease. Here the authors show that ULK1-mediated phosphorylation and PP2A-mediated dephosphorylation of ATG4 regulates its cellular activity to control LC3 processing.
format article
author N. Pengo
A. Agrotis
K. Prak
J. Jones
R. Ketteler
author_facet N. Pengo
A. Agrotis
K. Prak
J. Jones
R. Ketteler
author_sort N. Pengo
title A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
title_short A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
title_full A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
title_fullStr A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
title_full_unstemmed A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
title_sort reversible phospho-switch mediated by ulk1 regulates the activity of autophagy protease atg4b
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/be9d8c9445e94d1a89cc7a77d68e8daf
work_keys_str_mv AT npengo areversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT aagrotis areversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT kprak areversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT jjones areversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT rketteler areversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT npengo reversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT aagrotis reversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT kprak reversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT jjones reversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
AT rketteler reversiblephosphoswitchmediatedbyulk1regulatestheactivityofautophagyproteaseatg4b
_version_ 1718392283532886016