Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities.

Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Research Abstract Details 

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Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Abstract Text:

Bernat Crosas,John Hanna,Donald S Kirkpatrick,Dan Phoebe Zhang,Yoshiko Tone,Nathaniel A Hathaway,Christa Buecker,David S Leggett,Marion Schmidt,Randall W King,Steven P Gygi,Daniel Finley,

The ubiquitin ligase Hul5 was recently identified as a component of the proteasome, a multisubunit protease that degrades ubiquitin-protein conjugates. We report here a proteasome-dependent conjugating activity of Hul5 that endows proteasomes with the capacity to extend ubiquitin chains. hul5 mutants show reduced degradation of multiple proteasome substrates in vivo, suggesting that the polyubiquitin signal that targets substrates to the proteasome can be productively amplified at the proteasome. However, the products of Hul5 conjugation are subject to disassembly by a proteasome-bound deubiquitinating enzyme, Ubp6. A hul5 null mutation suppresses a ubp6 null mutation, suggesting that a balance of chain-extending and chain-trimming activities is required for proper proteasome function. As the association of Hul5 with proteasomes was found to be strongly stabilized by Ubp6, these enzymes may be situated in proximity to one another. We propose that through dynamic remodeling of ubiquitin chains, proteasomes actively regulate substrate commitment to degradation.

Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Publishing Authors By Initials

B Crosas,J Hanna,DS Kirkpatrick,DP Zhang,Y Tone,NA Hathaway,C Buecker,DS Leggett,M Schmidt,RW King,SP Gygi,D Finley,

For similar enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research abstracts see: enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research

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Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Cell

VOLUME: 127

Page Numbers: 1401-13

Journal Abbreviation: Cell

ISSN: 0092-8674

DAY: 29

MONTH: Dec

YEAR: 2006

Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Information

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LANGUAGE: eng

NlmUniqueID: 413066

Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Keywords Mesh Terms:

KEYWORDS: Ubiquitin-Protein Ligases

MESH TERMS: physiology

Chemical & Substance for Abstract: Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Information

Substance Name: Ubiquitin-Protein Ligases

Registry Number: EC 6.3.2.19

Grant and Affiliation Information for Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities.

AFFILIATION: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA; Institut de Biologia Molecular de Barcelona, CSIC, Jordi Girona 18-26, Barcelona 08034, Spain.

Country: United States

AGENCY: United States NIGMS

GRANT: GM67945

ACRONYM: GM

MEDLINETA: Cell

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