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Ubiquitin‐mediated proteolysis: biological regulation via destruction
Author(s) -
Ciechanover Aaron,
Orian Amir,
Schwartz Alan L.
Publication year - 2000
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(200005)22:5<442::aid-bies6>3.0.co;2-q
Subject(s) - ubiquitin , proteolysis , proteasome , microbiology and biotechnology , signal transduction , protein degradation , ubiquitin ligase , biology , ubiquitin conjugating enzyme , ubiquitin protein ligases , f box protein , biochemistry , chemistry , enzyme , gene
The ubiquitin proteolytic system plays an important role in a broad array of basic cellular processes. Among these are regulation of cell cycle, modulation of the immune and inflammatory responses, control of signal transduction pathways, development and differentiation. These complex processes are controlled via specific degradation of a single or a subset of proteins. Degradation of a protein by the ubiquitin system involves two successive steps, conjugation of multiple moieties of ubiquitin and degradation of the tagged protein by the 26S proteasome. An important question concerns the identity of the mechanisms that underlie the high degree of specificity of the system. Substrate recognition is governed by a large family ubiquitin ligases that recognize the substrates, bind them and catalyze/facilitate their interaction with ubiquitin. BioEssays 22:442—451, 2000. © 2000 John Wiley & Sons, Inc.