Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Wertheim cung cấp cho các bạn kiến thức về ngành y đề tài: Global approaches to understanding ubiquitination. | Review Global approaches to understanding ubiquitination Peter Kaiser and Lan Huang Addresses Department of Biological Chemistry School of Medicine Department of Physiology and Biophysics and Department of Developmental and Cell Biology University of California Irvine CA 92697-1700 USA. Correspondence Peter Kaiser. E-mail pkaiser@ Published 29 September 2005 Genome Biology 2005 6 233 doi gb-2005-6-l0-233 The electronic version of this article is the complete one and can be found online at http 2005 6 10 233 2005 BioMed Central Ltd Abstract Ubiquitination - the linkage of one or more molecules of the protein ubiquitin to another protein -regulates a wide range of biological processes in all eukaryotes. We review the proteome-wide strategies that are being used to study aspects of ubiquitin biology including substrates components of the proteasome and ubiquitin ligases and deubiquitination. Ubiquitin a small protein of 76 amino acids is highly conserved in all eukaryotes. In a multi-step process ubiquitin is covalently linked to lysine residues of substrate proteins. If a single molecule of ubiquitin is linked to a protein this is referred to as mono-ubiquitination a process that is of particular importance for protein trafficking but has also been shown to regulate retrovirus budding and to modulate protein function directly 1 . A lysine residue of a ubiquitin molecule attached to a substrate can itself serve as an acceptor for an additional ubiquitin molecule and this process can be repeated so that poly-ubiquitinated proteins form. Polyubiquitin chains serve as recognition signals for the 26S pro-teasome the major regulator of protein abundance in cells and poly-ubiquitination thus often initiates proteolysis of the substrate. But poly-ubiquitination can also regulate protein function directly without affecting stability in ways similar to mono-ubiquitination and other post-translational modifications. The mechanisms underlying .
