Proteolysis and the cell cycle.

Research output: Contribution to journalComment/debate

27 Citations (Scopus)

Abstract

Without doubt, one of the more dramatic breakthroughs in recent cell cycle history has been the discovery that growth regulators are controlled by proteolysis. This concept blossomed within the last six or seven years, but the story really began when cyclins were discovered, soon followed by the suggestion that proteolysis events might control cell cycle transitions. Proteolytic targets that are now known include most of the cyclins, cyclin dependent kinase inhibitors, DNA replication factors, the securin class of proteins that inhibit loss of sister chromatid cohesion following DNA replication and, of course, the cohesion factor itself. Protein degradation is controlled in various ways including ubiquitin-dependent targeting to proteasomes, activation of ubiquitin ligases by ubiquitin-like molecule conjugation, phosphorylation of proteolytic targets, and activation of the separin class of proteases.

Original languageEnglish (US)
Pages (from-to)233-234
Number of pages2
JournalCell cycle (Georgetown, Tex.)
Volume1
Issue number4
StatePublished - Jan 1 2002

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Proteolysis
Ubiquitin
Cell Cycle
Cyclins
Cells
DNA Replication
Securin
Chemical activation
Phosphorylation
Chromatids
Cyclin-Dependent Kinases
DNA
Proteasome Endopeptidase Complex
Ligases
Cell Cycle Checkpoints
Proteins
Peptide Hydrolases
History
Degradation
Molecules

Cite this

Proteolysis and the cell cycle. / Clarke, Duncan J.

In: Cell cycle (Georgetown, Tex.), Vol. 1, No. 4, 01.01.2002, p. 233-234.

Research output: Contribution to journalComment/debate

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