Abstract
The irreversible nature of mitotic entry is due to the activation of mitosis specific kinases such as cdk1/cyclin B. Cdk1/cyclin B induces activation of mitosis by promoting phosphatases while suppressing inhibitory factors such as the tyrosine kinase wee1. Since wee1 inactivates cdk1/cyclin B during the S and G2 phases, its activity must be downregulated for mitotic progression to occur. One mechanism of suppressing wee1 activity is ubiquitin-dependent proteolysis. Cdk1/cyclin B1 phosphorylates wee1, targeting it for recognition by ubiquitin ligases and subsequent proteasomal degradation. One of the ubiquitin ligases promoting wee1 destruction during mitosis is the SCFβ-trcp complex. We demonstrate that this complex, and a second SCF complex containing the F-box protein Tome-1, regulate wee1 degradation during the S and G2 phases of the cell cycle. Therefore, redundant ubiquitin ligase activities promote efficient mitotic entry of eukaryotic cells.
| Original language | English |
|---|---|
| Pages (from-to) | 2795-2799 |
| Number of pages | 5 |
| Journal | Cell Cycle |
| Volume | 6 |
| Issue number | 22 |
| State | Published - Nov 15 2007 |
| Externally published | Yes |
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Keywords
- β-TRCP
- Degradation
- F-box
- Mitosis
- Tome-1
- Wee1
ASJC Scopus subject areas
- Cell Biology
- Biochemistry
- Molecular Biology
Cite this
Redundant ubiquitin ligase activities regulate wee1 degradation and mitotic entry. / Smith, Anthony; Simanski, Scott; Fallahi, Mohammad; Ayad, Nagi.
In: Cell Cycle, Vol. 6, No. 22, 15.11.2007, p. 2795-2799.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Redundant ubiquitin ligase activities regulate wee1 degradation and mitotic entry
AU - Smith, Anthony
AU - Simanski, Scott
AU - Fallahi, Mohammad
AU - Ayad, Nagi
PY - 2007/11/15
Y1 - 2007/11/15
N2 - The irreversible nature of mitotic entry is due to the activation of mitosis specific kinases such as cdk1/cyclin B. Cdk1/cyclin B induces activation of mitosis by promoting phosphatases while suppressing inhibitory factors such as the tyrosine kinase wee1. Since wee1 inactivates cdk1/cyclin B during the S and G2 phases, its activity must be downregulated for mitotic progression to occur. One mechanism of suppressing wee1 activity is ubiquitin-dependent proteolysis. Cdk1/cyclin B1 phosphorylates wee1, targeting it for recognition by ubiquitin ligases and subsequent proteasomal degradation. One of the ubiquitin ligases promoting wee1 destruction during mitosis is the SCFβ-trcp complex. We demonstrate that this complex, and a second SCF complex containing the F-box protein Tome-1, regulate wee1 degradation during the S and G2 phases of the cell cycle. Therefore, redundant ubiquitin ligase activities promote efficient mitotic entry of eukaryotic cells.
AB - The irreversible nature of mitotic entry is due to the activation of mitosis specific kinases such as cdk1/cyclin B. Cdk1/cyclin B induces activation of mitosis by promoting phosphatases while suppressing inhibitory factors such as the tyrosine kinase wee1. Since wee1 inactivates cdk1/cyclin B during the S and G2 phases, its activity must be downregulated for mitotic progression to occur. One mechanism of suppressing wee1 activity is ubiquitin-dependent proteolysis. Cdk1/cyclin B1 phosphorylates wee1, targeting it for recognition by ubiquitin ligases and subsequent proteasomal degradation. One of the ubiquitin ligases promoting wee1 destruction during mitosis is the SCFβ-trcp complex. We demonstrate that this complex, and a second SCF complex containing the F-box protein Tome-1, regulate wee1 degradation during the S and G2 phases of the cell cycle. Therefore, redundant ubiquitin ligase activities promote efficient mitotic entry of eukaryotic cells.
KW - β-TRCP
KW - Degradation
KW - F-box
KW - Mitosis
KW - Tome-1
KW - Wee1
UR - http://www.scopus.com/inward/record.url?scp=37249063516&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37249063516&partnerID=8YFLogxK
M3 - Article
VL - 6
SP - 2795
EP - 2799
JO - Cell Cycle
JF - Cell Cycle
SN - 1538-4101
IS - 22
ER -