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The lysine48-based polyubiquitin chain proteasomal signal: not a single child anymore

Official URL:https://doi.org/10.1002/anie.201205656
PubMed:View item in PubMed
Creators Name:Kravtsova-Ivantsiv, Y. and Sommer, T. and Ciechanover, A.
Journal Title:Angewandte Chemie International Edition
Journal Abbreviation:Angew Chem Int Ed Engl
Volume:52
Number:1
Page Range:192-198
Date:2 January 2013
Keywords:Monoubiquitination, Polyubiquitin Chains, Proteasome, Protein Degradation, Ubiquitin
Abstract:The conjugation of ubiquitin (Ub) to proteins is involved in the regulation of many processes. The modification serves as a recognition element in trans, in which downstream effectors bind to the modified protein and determine its fate and/or function. A polyUb chain that is linked through internal lysine (Lys)-48 of Ub and anchored to an internal Lys residue of the substrate has become the accepted "canonical" signal for proteasomal targeting and degradation. However, recent studies show that the signal is far more diverse and that chains based on other internal linkages, as well as linear or heterologous chains made of Ub and Ub-like proteins and even monoUb, are recognized by the proteasome. In addition, chains linked to residues other than internal Lys were described, all challenging the current paradigm.
ISSN:1433-7851
Publisher:Wiley-VCH (Germany)
Item Type:Article

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