Ubiquitin superfolds: intrinsic and attachable regulators of cellular activities?
Ubiquitinylation, the post-translational covalent conjugation of ubiquitin to other proteins, mediates diverse cellular processes in addition to the proteasome-catalysed degradation signalled by multiple ubiquitinylation. Ubiquitin superfolds have also been found in other proteins. The amino acid sequences of these superfolds are unrelated to ubiquitin, but they have an almost identical three-dimensional shape to that of ubiquitin. Additionally, a number of 'ubiquitin-like' proteins, some of which can be conjugated to other proteins, may also contain the ubiquitin superfold. Intrinsic and attachable ubiquitin superfolds can act as powerful ligands and probably have important roles in protein-protein interactions in the cell.
Mayer
R J
RJ
Laboratory of Intracellular Proteolysis, Molecular and Cellular Biology Research Section, School of Biomedical Sciences, University of Nottingham Medical School, Queen's Medical Centre, Nottingham, NG7 2UH, UK. John.Mayer@nottingham.ac.uk
Landon
M
M
Layfield
R
R
D017510:Protein Folding; D015398:Signal Transduction; D014452:Ubiquitins / Q000737:chemistry / Q000378:metabolism*
D014452:Ubiquitins