title: Diversity of polyubiquitin chains.
abstract: Polyubiquitin chains linked through different lysines of ubiquitin may exert both proteasome-dependent and -independent functions. In a recent Cell issue, Xu et al. employ quantitative proteomics to profile polyubiquitin linkages in yeast. They find that linkages through all lysines of ubiquitin, except lysine-63, can target proteasomal degradation in vivo, and that lysine-11 polyubiquitination is important for endoplasmic reticulum-associated degradation (ERAD).
authors.affiliation: Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA.
authors.forename: Anirban
authors.initials: A
authors.lastname: Adhikari
authors.forename: Zhijian J
authors.initials: ZJ
authors.lastname: Chen
mesh_terms: D008239:Lysine / Q000378:metabolism; D025821:Polyubiquitin / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D054875:Ubiquitination
chemical_list: D025821:Polyubiquitin; D046988:Proteasome Endopeptidase Complex; D008239:Lysine