Linear ubiquitin chain-binding domains.
Ubiquitin modification (ubiquitination) of target proteins can vary with respect to chain lengths, linkage type, and chain forms, such as homologous, mixed, and branched ubiquitin chains. Thus, ubiquitination can generate multiple unique surfaces on a target protein substrate. Ubiquitin-binding domains (UBDs) recognize ubiquitinated substrates, by specifically binding to these unique surfaces, modulate the formation of cellular signaling complexes and regulate downstream signaling cascades. Among the eight different homotypic chain types, Met1-linked (also termed linear) chains are the only chains in which linkage occurs on a non-Lys residue of ubiquitin. Linear ubiquitin chains have been implicated in immune responses, cell death and autophagy, and several UBDs - specific for linear ubiquitin chains - have been identified. In this review, we describe the main principles of ubiquitin recognition by UBDs, focusing on linear ubiquitin chains and their roles in biology.
['Fennell|Lilian M|LM|', 'Rahighi|Simin|S|', 'Ikeda|Fumiyo|F|0000-0003-0407-2768']
D000818:Animals D001665:Binding Sites D020134:Catalytic Domain D004476:Ectodermal Dysplasia D006801:Humans D051550:I-kappa B Kinase D009154:Mutation D011485:Protein Binding D000072417:Protein Domains D011506:Proteins D025801:Ubiquitin D054875:Ubiquitination D016335:Zinc Fingers
ubiquitin ubiquitin-binding domain linear ubiquitin chain NZF UBAN