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.
Original language | English (US) |
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Article number | 10 |
Pages (from-to) | 157-164 |
Number of pages | 8 |
Journal | Methods in Enzymology |
Volume | 399 |
DOIs | |
State | Published - Jan 1 2005 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology