title: Analysis of ubiquitin chain-binding proteins by two-hybrid methods.
abstract: Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.
authors.affiliation: Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas, USA.
authors.forename: Jennifer
authors.initials: J
authors.lastname: Apodaca
authors.forename: Jungmi
authors.initials: J
authors.lastname: Ahn
authors.forename: Ikjin
authors.initials: I
authors.lastname: Kim
authors.forename: Hai
authors.initials: H
authors.lastname: Rao
mesh_terms: D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D020349:Surface Plasmon Resonance / Q000379:methods*; D020798:Two-Hybrid System Techniques; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D011506:Proteins; D025801:Ubiquitin