Ubiquitylation and cell signaling.
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.
Haglund
Kaisa
K
Institute for Biochemistry II, University Hospital of Goethe University, Frankfurt am Main, Germany.
Dikic
Ivan
I
D002467:Cell Nucleus / Q000378:metabolism; D004260:DNA Repair; D004261:DNA Replication / Q000502:physiology*; D005786:Gene Expression Regulation / Q000502:physiology*; D008954:Models, Biological; D016328:NF-kappa B / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000502:physiology; D011506:Proteins / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*; D014452:Ubiquitins / Q000378:metabolism*
D016328:NF-kappa B; D011506:Proteins; D014452:Ubiquitins