- Klaus-Peter KnobelochAffiliated withLeibniz-Institut für Molekulare Pharmakologie
Protein degradation; Posttranslational protein modification
Protein modification by the covalent attachment of ubiquitin chains serves as a signal to mark proteins for the degradation by a multicatalytic proteinase complex called the proteasome. Thus the ubiquitin proteasome system (UPS) controls the stability of proteins in a regulated manner affecting multiple essential cellular processes. In addition, dependent on the mode of linkage, ubiquitin regulates protein-protein interaction, endocytosis, replication and the formation of signaling complexes in a proteasome-independent fashion. Beside phosphorylation ubiquitination represents the most important posttranslational regulatory mechanism in biology.
Ubiquitin is a highly conserved 8.5 kDa polypeptide, which was first described in 1974. The discovery that the Ubiquitin proteasome system serves as a general mechanism to target proteins for destruct ...
Reference Work Entry Metrics
- Reference Work Title
- Encyclopedia of Molecular Pharmacology
- pp 1263-1266
- Print ISBN
- Online ISBN
- Springer Berlin Heidelberg
- Copyright Holder
- Springer-Verlag Berlin Heidelberg New York
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- Editor Affiliations
- 1. Pharmakologisches Institut, Universität Heidelberg
- 2. Institut für Pharmakologie, Freie Universität Berlin
- Author Affiliations
- 1. Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany
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