Cyclin is degraded by the ubiquitin pathway

• Published in: Nature (London) Vol. 349; no. 6305; pp. 132 - 138
• Main Authors: Glotzer, Michael, Murray, Andrew W, Kirschner, Marc W
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 10.01.1991; Nature Publishing Group
• Subjects: Amino Acid Sequence; Amino acids; Anaphase; Animals; Biochemistry; Biological and medical sciences; Cell cycle; Cell cycle, cell proliferation; Cell physiology; Cloning, Molecular; Conjugates; Cyclins - metabolism; Degradation; Fundamental and applied biological sciences. Psychology; Kinases; Kinetics; Mitosis; Molecular and cellular biology; Molecular Sequence Data; Physics; Protein synthesis; Proteins; Proteolysis; RNA, Messenger - metabolism; Ubiquitin; Ubiquitins - metabolism; Xenopus; Proteins; Ubiquitin; Vertebrata; Regulation(control); Proteolysis; Xenopus laevis; Cell cycle; Site directed mutagenesis; Amphibia; Molecular hybrid; Salientia; Molecular complex
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/349132a0

Cyclin degradation is the key step governing exit from mitosis and progress into the next cell cycle. When a region in the N terminus of cyclin is fused to a foreign protein, it produces a hybrid protein susceptible to proteolysis at mitosis. During the course of degradation, both cyclin and the hybrid form conjugates with ubiquitin. The kinetic properties of the conjugates indicate that cyclin is degraded by ubiquitin-dependent proteolysis. Thus anaphase may be triggered by the recognition of cyclin by the ubiquitin-conjugating system.