title: Protein-protein interactions regulate Ubl conjugation.
abstract: The ubiquitin-like proteins (Ubls) can be covalently linked to target proteins to provide a critical signal in diverse cellular processes. Members of the Ubl family include ubiquitin itself and a growing number of homologs such as SUMO, Nedd8, ISG15 and Atg8. The enzymatic mechanism of Ubl conjugation involves an E1, E2, E3 cascade of enzymes that is well conserved between the Ubls. In the past two years, novel structural details of Ubl conjugation were uncovered through analysis of protein-protein complexes. This has given insight in activation of E1, the role of the target lysine in E2-dependent catalysis, the role of noncovalent Ubl binding in Ubl chain formation and the importance of dimerization of Ring-type E3 ligases.
authors.affiliation: Division of Molecular Carcinogenesis, The Netherlands Cancer Institute and Center for Biomedical Genetics, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.
authors.forename: Puck
authors.initials: P
authors.lastname: Knipscheer
authors.forename: Titia K
authors.initials: TK
authors.lastname: Sixma
mesh_terms: D002384:Catalysis; D019281:Dimerization; D008958:Models, Molecular; D011485:Protein Binding; D014452:Ubiquitins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D014452:Ubiquitins