Document Detail


The ubiquitin-proteasome system of Saccharomyces cerevisiae.
MedLine Citation:
PMID:  23028185     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell.
Authors:
Daniel Finley; Helle D Ulrich; Thomas Sommer; Peter Kaiser
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Genetics     Volume:  192     ISSN:  1943-2631     ISO Abbreviation:  Genetics     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-02     Completed Date:  2013-04-09     Revised Date:  2013-10-09    
Medline Journal Info:
Nlm Unique ID:  0374636     Medline TA:  Genetics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  319-60     Citation Subset:  IM    
Affiliation:
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / genetics,  metabolism
Cell Cycle Proteins / genetics,  metabolism
Membrane Proteins / genetics,  metabolism
Proteasome Endopeptidase Complex / genetics*,  ultrastructure
Protein Processing, Post-Translational / genetics
Protein Transport*
Proteolysis
Saccharomyces cerevisiae* / genetics,  metabolism
Substrate Specificity
Ubiquitin* / genetics,  physiology
Ubiquitination / genetics
Grant Support
ID/Acronym/Agency:
CA112560/CA/NCI NIH HHS; GM095526/GM/NIGMS NIH HHS; GM43601/GM/NIGMS NIH HHS; GM66164/GM/NIGMS NIH HHS; R01 GM066164/GM/NIGMS NIH HHS; R37 GM043601/GM/NIGMS NIH HHS; //Cancer Research UK
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Membrane Proteins; 0/Ubiquitin; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/CDC48 protein
Comments/Corrections

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