The Ubiquitin–Proteasome System of Saccharomyces cerevisiae
Author(s) -
Daniel Finley,
Helle D. Ulrich,
Thomas Sommer,
Peter Kaiser
Publication year - 2012
Publication title -
genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.792
H-Index - 246
eISSN - 1943-2631
pISSN - 0016-6731
DOI - 10.1534/genetics.112.140467
Subject(s) - ubiquitin , proteasome , biology , saccharomyces cerevisiae , ubiquitin ligase , ubiquitin protein ligases , function (biology) , f box protein , ubiquitins , ubiquitin conjugating enzyme , microbiology and biotechnology , protein degradation , computational biology , genetics , biochemistry , yeast , gene
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.
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