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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Format: | Article |
Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3319606?pdf=render |
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author | Lynn Burchell Viduth K Chaugule Helen Walden |
author_facet | Lynn Burchell Viduth K Chaugule Helen Walden |
author_sort | Lynn Burchell |
collection | DOAJ |
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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format | Article |
id | doaj.art-d0daaec419f54ab891600efb7b7a9df2 |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-12-22T06:58:25Z |
publishDate | 2012-01-01 |
publisher | Public Library of Science (PLoS) |
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series | PLoS ONE |
spelling | doaj.art-d0daaec419f54ab891600efb7b7a9df22022-12-21T18:34:53ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0174e3474810.1371/journal.pone.0034748Small, N-terminal tags activate Parkin E3 ubiquitin ligase activity by disrupting its autoinhibited conformation.Lynn BurchellViduth K ChauguleHelen WaldenParkin 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.http://europepmc.org/articles/PMC3319606?pdf=render |
spellingShingle | Lynn Burchell Viduth K Chaugule Helen Walden Small, N-terminal tags activate Parkin E3 ubiquitin ligase activity by disrupting its autoinhibited conformation. PLoS ONE |
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 |
url | http://europepmc.org/articles/PMC3319606?pdf=render |
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