Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation

Parkin is an E3 ubiquitin ligase, mutations in which cause Autosomal Recessive Parkinson's Disease. Many studies aimed at understanding Parkin function, regulation and dysfunction are performed using N-terminal epitope tags. We report here that the use of small tags such as FLAG, cMyc and HA, i...

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Detalles Bibliográficos
Autores principales: Burchell, Lynn, Chaugule, Viduth K., Walden, Helen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3319606/
https://www.ncbi.nlm.nih.gov/pubmed/22496854
http://dx.doi.org/10.1371/journal.pone.0034748
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author Burchell, Lynn
Chaugule, Viduth K.
Walden, Helen
author_facet Burchell, Lynn
Chaugule, Viduth K.
Walden, Helen
author_sort Burchell, Lynn
collection PubMed
description Parkin is an E3 ubiquitin ligase, mutations in which cause Autosomal Recessive Parkinson's Disease. Many studies aimed at understanding Parkin function, regulation and dysfunction are performed using N-terminal epitope tags. We report here that the use of small tags such as FLAG, cMyc and HA, influence the physical stability and activity of Parkin in and out of cells, perturbing the autoinhibited native state of Parkin, resulting in an active-for-autoubiquitination species.
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spelling pubmed-33196062012-04-11 Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation Burchell, Lynn Chaugule, Viduth K. Walden, Helen PLoS One Research Article Parkin is an E3 ubiquitin ligase, mutations in which cause Autosomal Recessive Parkinson's Disease. Many studies aimed at understanding Parkin function, regulation and dysfunction are performed using N-terminal epitope tags. We report here that the use of small tags such as FLAG, cMyc and HA, influence the physical stability and activity of Parkin in and out of cells, perturbing the autoinhibited native state of Parkin, resulting in an active-for-autoubiquitination species. Public Library of Science 2012-04-04 /pmc/articles/PMC3319606/ /pubmed/22496854 http://dx.doi.org/10.1371/journal.pone.0034748 Text en Burchell et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Burchell, Lynn
Chaugule, Viduth K.
Walden, Helen
Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation
title Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation
title_full Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation
title_fullStr Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation
title_full_unstemmed Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation
title_short Small, N-Terminal Tags Activate Parkin E3 Ubiquitin Ligase Activity by Disrupting Its Autoinhibited Conformation
title_sort small, n-terminal tags activate parkin e3 ubiquitin ligase activity by disrupting its autoinhibited conformation
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3319606/
https://www.ncbi.nlm.nih.gov/pubmed/22496854
http://dx.doi.org/10.1371/journal.pone.0034748
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