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PMID: 17418826 Published · ppublish English Journal Article Review

A proteasome for all occasions.

FEBS letters ·Vol. 581 ·No. 15 ·2007-06-19 ·Pages 2854-61

Hanna J, Finley D

Abstract

In the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent modification by ubiquitin, and are subsequently destroyed by the proteasome. Traditionally, 26S proteasomes have been seen as largely uniform in their composition and functional capacity. Accordingly, cells can control proteasome abundance via transcriptional pathways that mediate concerted regulation of all known proteasome genes. However, recent evidence suggests that the proteasome is also subject to subunit-specific modes of regulation, which serve to alter proteasome function and may generate ensembles of compositionally distinct proteasomes. These modes of proteasome regulation provide varied means to adapt protein degradation pathways to changing conditions in the cell.

MeSH Terms
Animals Arsenites/toxicity DNA-Binding Proteins/genetics,metabolism Endopeptidases/genetics,metabolism Humans Models, Biological Models, Molecular Multiprotein Complexes Proteasome Endopeptidase Complex/chemistry,genetics,metabolism RNA-Binding Proteins/genetics,metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins/genetics,metabolism Transcription Factors/genetics,metabolism Transcriptional Activation Ubiquitin/metabolism
Chemicals
Arsenites DNA-Binding Proteins Multiprotein Complexes RNA-Binding Proteins RPN4 protein, S cerevisiae Saccharomyces cerevisiae Proteins Transcription Factors Ubiquitin Endopeptidases Proteasome Endopeptidase Complex UBP6 protein, S cerevisiae arsenite
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hanna John
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Finley Daniel
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Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
DOI
10.1016/j.febslet.2007.03.053
Published
2007-06-19
Epub
2007-00-30
Pages
2854-61
Language
English
Region
England
NLM ID
0155157
PMCID
PMC1965587
Subset
IM
Grants
NIGMS NIH HHS · R01 GM065592 · United States
NIGMS NIH HHS · R01 GM065592-04 · United States
External Links
PubMed source DOI: 10.1016/j.febslet.2007.03.053 PMC Full Text View journal details
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