ParkinsonCanadaV1, Main, Exploration, bibRecord, 001718

Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*

Identifieur interne : 001718 ( Main/Exploration ); précédent : 001717; suivant : 001719

Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*

Auteurs : Thomas M. Durcan ; Maria Kontogiannea ; Nathalie Bedard ; Simon S. Wing ; Edward A. Fon

Source :

The Journal of Biological Chemistry [ 0021-9258 ] ; 2011.

RBID : PMC:3249107

English descriptors

KwdEn :
- Animals, Ataxin-3, Catalytic Domain, HEK293 Cells, Humans, Mice, Nuclear Proteins (chemistry), Nuclear Proteins (metabolism), Protein Stability, Transcription Factors (chemistry), Transcription Factors (metabolism), Ubiquitin-Conjugating Enzymes (metabolism), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
MESH :
- chemical , chemistry : Nuclear Proteins, Transcription Factors.
- chemical , metabolism : Nuclear Proteins, Transcription Factors, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases.
- chemical : Ataxin-3.
- Animals, Catalytic Domain, HEK293 Cells, Humans, Mice, Protein Stability, Ubiquitination.

Abstract

Background: The deubiquitinating enzyme (DUB) ataxin-3 opposes the E3 ubiquitin-ligase activity of parkin, however, the mechanism involved is unclear.

Results: Ataxin-3 opposes parkin ubiquitination by regulating the E2 ubiquitin-conjugating enzyme.

Conclusion: The components within a E2·E3·DUB complex are functionally coupled to fine-tune the overall extent of ubiquitination.

Significance: The work broadens our understanding of the intricate interplay between E3s, DUBs, and the ubiquitination machinery.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3249107

DOI: 10.1074/jbc.M111.288449
PubMed: 22081612
PubMed Central: 3249107

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
 The deubiquitinating enzyme (DUB) ataxin-3 opposes the E3 ubiquitin-ligase activity of parkin, however, the mechanism involved is unclear.</p>
<p><bold>Results:</bold>
 Ataxin-3 opposes parkin ubiquitination by regulating the E2 ubiquitin-conjugating enzyme.</p>
<p><bold>Conclusion:</bold>
 The components within a E2·E3·DUB complex are functionally coupled to fine-tune the overall extent of ubiquitination.</p>
<p><bold>Significance:</bold>
 The work broadens our understanding of the intricate interplay between E3s, DUBs, and the ubiquitination machinery.</p>
</div>
</front>
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<name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M." last="Durcan">Thomas M. Durcan</name>
<name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A." last="Fon">Edward A. Fon</name>
<name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name>
<name sortKey="Wing, Simon S" sort="Wing, Simon S" uniqKey="Wing S" first="Simon S." last="Wing">Simon S. Wing</name>
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La maladie de Parkinson au Canada (serveur d'exploration)

Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*

Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*

Source :

English descriptors

Abstract

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	La maladie de Parkinson au Canada (serveur d'exploration)
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