How does the ubiquitin system selectively target proteins for degradation? This review explores the ubiquitin system, focusing on the selective degradation of short-lived proteins in eukaryotic cells. This pathway targets proteins for degradation via covalent ligation to ubiquitin, a conserved small protein. Ubiquitin-mediated degradation plays roles in cell-cycle progression, signal transduction, transcription, receptor down-regulation, and endocytosis. The ubiquitin system has implications in the immune response, development, and programmed cell death. Abnormalities in ubiquitin-mediated processes can cause pathological conditions, including malignant transformation. This review discusses recent information on functions and mechanisms of the ubiquitin system. It focuses on the mode of action of ubiquitin-protein ligation systems and the signals recognized by these systems. This comprehensive view of the ubiquitin system is vital for understanding various cellular processes and disease mechanisms.
Published in the Annual Review of Biochemistry, this article reviews the ubiquitin system. It fits the journal's focus on providing comprehensive overviews of key topics in biochemistry. The selectivity of protein degradation is determined mainly at the stage of ligation to ubiquitin. Analysis of the references and citations would likely reveal how the review connects to a range of research in cell biology, genetics, and disease mechanisms.
| Category | Category Repetition |
|---|---|
| Science: Biology (General) | 2,442 |
| Science: Chemistry: Organic chemistry: Biochemistry | 1,839 |
| Science: Biology (General): Cytology | 1,413 |
| Science: Biology (General): Genetics | 1,362 |
| Medicine: Medicine (General) | 650 |