The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains

Phosphorylated ubiquitin produced by PINK1 kinase functions as a PARK2/Parkin activator by derepressing intramolecular autoinhibition of PARK2 E3 activity. Unexpectedly, we revealed that phosphorylated polyubiquitin chain also functions in the PARK2 recruitment process as a PARK2 receptor. Phosphory...

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Detalles Bibliográficos
Autores principales: Matsuda, Noriyuki, Tanaka, Keiji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Autophagic Punctum
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4590609/
https://www.ncbi.nlm.nih.gov/pubmed/26213095
http://dx.doi.org/10.1080/15548627.2015.1071760
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author Matsuda, Noriyuki
Tanaka, Keiji
author_facet Matsuda, Noriyuki
Tanaka, Keiji
author_sort Matsuda, Noriyuki
collection PubMed
description Phosphorylated ubiquitin produced by PINK1 kinase functions as a PARK2/Parkin activator by derepressing intramolecular autoinhibition of PARK2 E3 activity. Unexpectedly, we revealed that phosphorylated polyubiquitin chain also functions in the PARK2 recruitment process as a PARK2 receptor. Phosphorylated ubiquitin enables us to comprehensively understand how PINK1 and PARK2 catalyzes (phospho-)ubiquitination of depolarized mitochondria and subsequent mitophagy.
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spelling pubmed-45906092016-02-03 The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains Matsuda, Noriyuki Tanaka, Keiji Autophagy Autophagic Punctum Phosphorylated ubiquitin produced by PINK1 kinase functions as a PARK2/Parkin activator by derepressing intramolecular autoinhibition of PARK2 E3 activity. Unexpectedly, we revealed that phosphorylated polyubiquitin chain also functions in the PARK2 recruitment process as a PARK2 receptor. Phosphorylated ubiquitin enables us to comprehensively understand how PINK1 and PARK2 catalyzes (phospho-)ubiquitination of depolarized mitochondria and subsequent mitophagy. Taylor & Francis 2015-07-25 /pmc/articles/PMC4590609/ /pubmed/26213095 http://dx.doi.org/10.1080/15548627.2015.1071760 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Autophagic Punctum
Matsuda, Noriyuki
Tanaka, Keiji
The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
title The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
title_full The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
title_fullStr The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
title_full_unstemmed The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
title_short The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
title_sort park2/parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains
topic Autophagic Punctum
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4590609/
https://www.ncbi.nlm.nih.gov/pubmed/26213095
http://dx.doi.org/10.1080/15548627.2015.1071760
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