Cdc25B activity is regulated by 14-3-3

Forrest, Alistair R.R.; Gabrielli, Brian

doi:10.1038/sj.onc.1204574

Cited by 97 publications

(76 citation statements)

References 41 publications

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“…Accumulated circumstantial evidence indicates that 14-3-3 negatively controls the G 2 /M transition by binding to Cdc25 through providing scaffolding or a cover that hides specific motifs, such as nuclear localization signal (NLS) or nuclear export signal (NES). Binding of 14-3-3 to Cdc25B was previously reported to induce the redistribution of Cdc25B from the nucleus to the cytoplasm and might contribute to stall the cell cycle at the G 2 phase after DNA damage (Davezac et al, 2000;Mils et al, 2000;Forrest and Gabrielli, 2001;Uchida et al, 2004). The amino acid residue essential for this effect was shown to be Ser323 of Cdc25B3 (or Cdc25B2; Davezac et al, 2000;Forrest and Gabrielli, 2001), which is the equivalent site to mouse Cdc25B-S321.…”

Section: Discussionmentioning

confidence: 93%

“…Binding of 14-3-3 to Cdc25B was previously reported to induce the redistribution of Cdc25B from the nucleus to the cytoplasm and might contribute to stall the cell cycle at the G 2 phase after DNA damage (Davezac et al, 2000;Mils et al, 2000;Forrest and Gabrielli, 2001;Uchida et al, 2004). The amino acid residue essential for this effect was shown to be Ser323 of Cdc25B3 (or Cdc25B2; Davezac et al, 2000;Forrest and Gabrielli, 2001), which is the equivalent site to mouse Cdc25B-S321. Studies of the interaction between Cdc25B and 14-3-3 clearly demonstrated that the binding of 14-3-3 masks the NLS of Cdc25B, thereby causing nuclear exclusion of the protein without affecting its phosphatase activity.…”

Section: Discussionmentioning

confidence: 93%

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Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Zhang

et al. 2008

Developmental Dynamics

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Protein kinase A (PKA) play a critical role in maintaining the meiotic arrest. However, the steps downstream of PKA remain largely unknown. In this study, we investigated the regulation of meiotic resumption by PKA/Cdc25B pathway in mouse oocytes. Injection of mRNA coding for Cdc25b-S321A had a more potent maturation-inducing ability than Cdc25b-WT. When co-injected with PKA inhibitor, Cdc25B-WT had similar activities with Cdc25B-S321A. Meanwhile, the phosphorylation of Cdc25B-S321 was detected in germinal vesicle (GV) oocytes by Western blotting with a phospho-Ser321-specific antibody and the band disappeared when oocytes reenter into the meiotic cell cycle. Furthermore, Cdc25B-WT translocated to the nucleus shortly before GV breakdown (GVBD), whereas phosphorylated Cdc25B-S321 expressed exclusively in the cytoplasm and the signal could not be detected in GVBD oocytes. Taken together, these data indicate that Cdc25B-Serine321 is the potential PKA target and Cdc25B subcellular localization determines its function during the process of maintaining GV arrest in mouse oocytes. Developmental Dynamics 237: 3777-3786, 2008.

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Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 93%

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Zhang

et al. 2008

Developmental Dynamics

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“…The ATM-Chk2 pathway was originally also suggested to be involved in the degradation of Cdc25A (Falck et al, 2001); however the finding that IR-induced degradation of Cdc25A in HCT116-Chk2 À/À cells occurs with the same kinetics as in wt-HCT116 cells indicates that the contribution of Chk2 to degradation of Cdc25A is either functionally redundant or occurs in a cell type-specific manner (Jin et al, 2008). In addition, Cdc25B and Cdc25C are phosphorylated by Chk1/2 at Ser-323 and Ser-216, respectively, and are functionally inactivated by binding to 14-3-3 proteins (Peng et al, 1997;Sanchez et al, 1997;Forrest and Gabrielli, 2001). Nonetheless, mice deficient in Cdc25B and Cdc25C are still able to fully activate the DNAdamage checkpoints, indicating that mere regulation of Cdc25A is sufficient to establish the checkpoint (Ferguson et al, 2005).…”

Section: Checkpoint Kinases-effectors Of the Checkpointmentioning

confidence: 92%

Checkpoint control and cancer

2011

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DNA-damaging therapies represent the most frequently used non-surgical anticancer strategies in the treatment of human tumors. These therapies can kill tumor cells, but at the same time they can be particularly damaging and mutagenic to healthy tissues. The efficacy of DNAdamaging treatments can be improved if tumor cell death is selectively enhanced, and the recent application of poly-(ADP-ribose) polymerase inhibitors in BRCA1/2-deficient tumors is a successful example of this. DNA damage is known to trigger cell-cycle arrest through activation of DNA-damage checkpoints. This arrest can be reversed once the damage has been repaired, but irreparable damage can promote apoptosis or senescence. Alternatively, cells can reenter the cell cycle before repair has been completed, giving rise to mutations. In this review we discuss the mechanisms involved in the activation and inactivation of DNA-damage checkpoints, and how the transition from arrest and cell-cycle re-entry is controlled. In addition, we discuss recent attempts to target the checkpoint in anticancer strategies.

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“…To test whether the levels of the key mitotic inducer Cyclin B1 was a limiting factor for checkpoint recovery in Wip1-depleted cells, we microinjected YFP-Cdc25B3 S323G, a potent activator of Cyclin B1-Cdk1 even in the presence of an active DNA damage checkpoint (Forrest and Gabrielli, 2001). Whereas injection of YFP-Cdc25B3 S323G resulted in efficient mitotic entry in DNA-damaged control cells, it failed to promote mitosis in Wip1-depleted cells.…”

Section: Wip1 Antagonizes P53-mediated Repression Of Mitotic Regulatorsmentioning

confidence: 99%

Wip1 confers G2 checkpoint recovery competence by counteracting p53-dependent transcriptional repression

Lindqvist

Bruijn

Macůrek

et al. 2009

EMBO J

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Activation of the DNA damage checkpoint causes a cellcycle arrest through inhibition of cyclin-dependent kinases (cdks). To successfully recover from the arrest, a cell should somehow be maintained in its proper cell-cycle phase. This problem is particularly eminent when a cell arrests in G2, as cdk activity is important to establish a G2 state. Here, we identify the phosphatase Wip1 (PPM1D) as a factor that maintains a cell competent for cell-cycle reentry during an ongoing DNA damage response in G2. We show that Wip1 function is required throughout the arrest, and that Wip1 acts by antagonizing p53-dependent repression of crucial mitotic inducers, such as Cyclin B and Plk1. Our data show that the primary function of Wip1 is to retain cellular competence to divide, rather than to silence the checkpoint to promote recovery. Our findings uncover Wip1 as a first in class recovery competence gene, and suggest that the principal function of Wip1 in cellular transformation is to retain proliferative capacity in the face of oncogene-induced stress.

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Cdc25B activity is regulated by 14-3-3

Cited by 97 publications

References 41 publications

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Checkpoint control and cancer

Wip1 confers G2 checkpoint recovery competence by counteracting p53-dependent transcriptional repression

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