Atypical ubiquitination of proteins


1. Institute of Biomedical Chemistry, Moscow, Russia
Type: Review
DOI: 10.18097/PBMC20166205496      UDK: 57.052      PubMed Id: 27797324
Year: 2016 vol: 62  issue:5  pages: 496-509
Abstract: Ubiquitination is a type of posttranslational modification of intracellular proteins characterized by covalent attachment of one (monoubiquitination) or several (polyubiquitination) of ubiquitin molecules to target proteins. In the case of polyubiquitination, linear or branched polyubiquitin chains are formed. Their formation involves various lysine residues of monomeric ubiquitin. The best studied is Lys48-polyubiquitination, which targets proteins for proteasomal degradation. In this review we have considered examples of so-called atypical polyubiquitination, which mainly involves other lysine residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys63) and also N-terminal methionine. The considered examples convincingly demonstrate that polyubiquitination of proteins not necessarily targets proteins for their proteolytic degradation in proteasomes. Atypically polyubiquitinated proteins are involved in regulation of various processes and altered polyubiquitination of certain proteins is crucial for development of serious diseases.
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Reference: Buneeva O.A., Medvedev A.E., Atypical ubiquitination of proteins, Biomeditsinskaya khimiya, 2016, vol: 62(5), 496-509.
This paper is also available as the English translation:10.1134/S1990750817010024