New EMBO Members Review
- The EMBO Journal (2005) 24, 3353 - 3359
- doi:10.1038/sj.emboj.7600808
Published online: 8 September 2005
Subject Categories:
Ubiquitylation and cell signaling
Kaisa Haglund1 and Ivan Dikic1,2
- Institute for Biochemistry II, University Hospital of Goethe University, Frankfurt am Main, Germany
- Mediterranean Institute for Life Sciences (MedILS), Split, Croatia
Correspondence to:
Ivan Dikic, Institute for Biochemistry II, University Hospital of Goethe University, Theodor-Stern-Kai 7, Frankfurt am Main, 60590, Germany. Tel: +49 69 6301 83647; Fax: +49 69 6301 5577; E-mail: Ivan.Dikic@biochem2.de
Received 22 June 2005; Accepted 18 August 2005
Abstract
Ubiquitylation is an emerging mechanism implicated in a variety of nonproteolytic cellular functions. The attachment of a single ubiquitin (Ub) or poly-Ub (lysine 63) chains to proteins control gene transcription, DNA repair and replication, intracellular trafficking and virus budding. In these processes, protein ubiquitylation exhibits inducibility, reversibility and recognition by specialized domains, features similar to protein phosphorylation, which enable Ub to act as a signaling device. Here, we highlight several recent examples on how Ub regulates signaling and how signaling regulates ubiquitylation during physiological and pathological cellular processes.
Keywords:
- endocytosis,
- NF-
B, - receptor tyrosine kinase,
- signal transduction,
- ubiquitin
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