Studies of the ubiquitin proteasome system.
A concept that has arisen over the last decade is that proteins can, in general, be covalently modified by polypeptides, resulting in alterations in their fate and function. The first-identified and most well studied of these modifying polypeptides is ubiquitin. Although targeting for proteasomal degradation is the best studied outcome of ubiquitylation, we now understand that modification of proteins with ubiquitin has numerous other cellular roles that alter protein function and that are unrelated to proteasomal degradation. Ubiquitylation is a complex process that is regulated at the level of both addition and removal of ubiquitin from target proteins. This unit includes a number of different basic protocols that will facilitate the study of components of the ubiquitin system and substrate ubiquitylation both in vitro and in cells. Because another protein modifier, NEDD8, itself regulates aspects of the ubiquitin system, basic protocols on neddylation are also included in this unit.
Lorick
Kevin L
KL
National Cancer Institute, Frederick, Maryland, USA.
Yang
Yili
Y
Jensen
Jane P
JP
Iwai
Kazuhiro
K
Weissman
Allan M
AM
D000818:Animals; D046988:Proteasome Endopeptidase Complex / Q000032:analysis*; D011817:Rabbits; D025801:Ubiquitin / Q000032:analysis*; D044764:Ubiquitin-Activating Enzymes / Q000032:analysis; D044763:Ubiquitin-Conjugating Enzymes / Q000032:analysis; D043743:Ubiquitin-Protein Ligase Complexes / Q000032:analysis; D044767:Ubiquitin-Protein Ligases / Q000032:analysis; D054875:Ubiquitination
D025801:Ubiquitin; D044763:Ubiquitin-Conjugating Enzymes; D043743:Ubiquitin-Protein Ligase Complexes; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex; D044764:Ubiquitin-Activating Enzymes