Ubiquitylation is emerging as a versatile device for controlling cellular functions. Here, we propose that monoubiquitylation is rapidly induced by signalling events and allows the establishment of protein-protein interactions between monoubiquitylated proteins and partners that contain distinct ubiquitin-binding domains. We also put forward speculative models for the regulation of monoubiquitylation versus polyubiquitylation.
|Number of pages||7|
|Journal||Nature Reviews Molecular Cell Biology|
|Publication status||Published - Jun 1 2003|
ASJC Scopus subject areas
- Cell Biology
- Molecular Biology