Role of ubiquitin- and Ubl-binding proteins in cell signaling.
Besides tagging proteins for degradation, ubiquitin is now recognized as a signaling module for diverse cellular processes, including progression through the cell cycle, DNA repair, gene transcription, receptor trafficking and endocytosis. Recent advances have indicated the existence of a wide variety of ubiquitin-binding proteins that, upon recognition of conjugated ubiquitin moieties, can control assembly of complex signaling networks. Small ubiquitin-like proteins, like SUMO, emerge to play biological roles distinct from ubiquitin, and require specific recognition by a dedicated set of proteins. Identification and characterization of recognition motifs and domains for ubiquitin-like proteins have just begun, promising new insights into the diversity of functions ubiquitin family proteins have in physiological and pathological settings.
Kirkin
Vladimir
V
Institute of Biochemistry II, Goethe University Hospital, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany.
Dikic
Ivan
I
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D004260:DNA Repair; D004705:Endocytosis; D006801:Humans; D008954:Models, Biological; D025842:SUMO-1 Protein / Q000378:metabolism*; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology*; D014158:Transcription, Genetic; D025801:Ubiquitin / Q000235:genetics / Q000378:metabolism*; D014452:Ubiquitins / Q000378:metabolism*
D002352:Carrier Proteins; D025842:SUMO-1 Protein; D025801:Ubiquitin; D014452:Ubiquitins