To be or not to be ubiquitinated?
Levels of p21, a cyclin-dependent kinase (CDK) inhibitor, are controlled in part at the post-translational level by protein degradation. Although the signaling pathways leading to p21 degradation have not yet been fully elucidated, it is evident that p21 ubiquitination is an essential factor in its degradation. We discuss that, with the only notable exception of ornithine decarboxylase, ubiquitination appears to be a prerequisite for proteasomal degradation rather than an unnecessary byproduct of such proteolysis.
Bloom
Joanna
J
Department of Pathology and NYU Cancer Institute, New York University School of Medicine, New York, New York 10016, USA.
Pagano
Michele
M
D000818:Animals; D002453:Cell Cycle / Q000502:physiology; D050759:Cyclin-Dependent Kinase Inhibitor p21; D016213:Cyclins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011489:Protein Denaturation / Q000502:physiology; D011817:Rabbits; D015398:Signal Transduction / Q000502:physiology; D014452:Ubiquitins / Q000378:metabolism*; D014466:Ultraviolet Rays
D050759:Cyclin-Dependent Kinase Inhibitor p21; D016213:Cyclins; D009097:Multienzyme Complexes; D014452:Ubiquitins; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex