Interwoven ubiquitination oscillators and control of cell cycle transitions.

Xiaolu Cambronne, J. Wade Harper

Research output: Contribution to journalReview article

39 Citations (Scopus)

Abstract

Ubiquitin-mediated proteolysis has emerged as a paramount mechanism for regulating the cell division cycle. Changes in the activities of certain E3 ligases can promote the interconversion of cell cycle states or transitions. Recent studies have revealed how distinct E3 ligases control the activity of other E3 ligases and how the interplay between these degradation machines sets up the timing of cell cycle transitions. For example, during G1, the anaphase-promoting complex in conjunction with Cdh1 (APC(Cdh1)) catalyzes destruction of the S-phase activator Skp2, helping to define the G1 state. In response to poorly defined signals, APC(Cdh1) activity is reduced, allowing accumulation of Skp2 and therefore entry into S phase. In many cases, E3 ligases also function to ubiquitinate proteins that negatively regulate cell cycle transitions. Recent work indicates that cyclin-dependent kinase 2 and Polo kinase collaborate to phosphorylate Wee1, thereby promoting its ubiquitination by SCF(beta-TRCP). Thus, activation of the mitotic transition produces feedback signals that help to turn off the negative upstream pathway to further reenforce the transition.

Original languageEnglish (US)
JournalScience's STKE : signal transduction knowledge environment
Volume2004
Issue number242
StatePublished - Jan 1 2004
Externally publishedYes

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Ubiquitin-Protein Ligases
Ubiquitination
Cell Cycle Checkpoints
Cell Cycle
Cells
Anaphase-Promoting Complex-Cyclosome
S Phase
Cyclin-Dependent Kinase 2
Proteolysis
Ubiquitin
Phosphotransferases
Chemical activation
Feedback
Degradation
Proteins

Cite this

Interwoven ubiquitination oscillators and control of cell cycle transitions. / Cambronne, Xiaolu; Harper, J. Wade.

In: Science's STKE : signal transduction knowledge environment, Vol. 2004, No. 242, 01.01.2004.

Research output: Contribution to journalReview article

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