title: From UBA to UBX: new words in the ubiquitin vocabulary.
abstract: Ubiquitination is a versatile tool of eukaryotic cells for controlling the stability, function and subcellular localization of proteins. The variety of cellular processes regulated by ubiquitination demands high substrate specificity of the ubiquitination machinery as well as the existence of diverse downstream effector proteins interacting with ubiquitinated substrates. Most of these cellular effectors are characterized by a modular composition of ubiquitin-binding motifs and further domains mediating specific functions. Here, I give an overview of important ubiquitin-related protein motifs, including the UBA, UIM, UBD and UBX domains, and propose a model for the role of subclasses of UBA-domain-containing proteins in ubiquitin-mediated proteolysis.
authors.affiliation: Dept of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany. buchberg@biochem.mpg.de
authors.forename: Alexander
authors.initials: A
authors.lastname: Buchberger
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006801:Humans; D009097:Multienzyme Complexes / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D012568:Schizosaccharomyces; D013379:Substrate Specificity; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009097:Multienzyme Complexes; D025801:Ubiquitin; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex