Document Detail


Proteasomal recognition of ubiquitylated substrates.
MedLine Citation:
PMID:  20399133     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ubiquitin/26S proteasome-mediated proteolysis controls the half-life of numerous critical regulatory proteins and is an intimate regulatory component for nearly all aspects of cellular processes. In addition to ubiquitin conjugation, an additional level of substrate specificity is regulated at the step of proteasomal recognition of ubiquitylated substrates, which serves as an important mechanistic and regulatory component to connect the substrate from the conjugation machinery to the 26S proteasome. In this review, we discuss current knowledge and future challenges relevant to understanding the mechanism, regulation, functions and substrate specificity of proteasomal recognition mediated by a multitude of ubiquitin receptors. The mechanistic details of major recognition pathways for ubiquitylated substrates are clearly divergent within and across species, which implies functional differentiation.
Authors:
Hongyong Fu; Ya-Ling Lin; A S Fatimababy
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2010-04-14
Journal Detail:
Title:  Trends in plant science     Volume:  15     ISSN:  1878-4372     ISO Abbreviation:  Trends Plant Sci.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-05     Completed Date:  2010-09-01     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9890299     Medline TA:  Trends Plant Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  375-86     Citation Subset:  IM    
Affiliation:
Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan 115, ROC. hongyong@gate.sinica.edu.tw
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MeSH Terms
Descriptor/Qualifier:
Animals
Humans
Proteasome Endopeptidase Complex / metabolism*
Protein Binding
Signal Transduction
Substrate Specificity
Ubiquitination*
Chemical
Reg. No./Substance:
EC 3.4.25.1/Proteasome Endopeptidase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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