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Myelodysplastic syndrome -related P95 (show NBN Proteins) point mutants of SRSF2 (show SRSF2 Proteins) lead to alternative splicing of CDC25C in a manner that is not dependent on the DNA damage response.
The aim of this review is to shed light on the role of four different phosphatases (PTEN, PP2A (show PPP2R4 Proteins), CDC25 (show RASGRF1 Proteins) and DUSP1 (show DUSP1 Proteins)) in five different solid tumors (breast cancer, lung cancer, pancreatic cancer, prostate cancer and ovarian cancer), in order to better understand the most frequent and aggressive primary cancer of the central nervous system, glioblastoma.
Data show that TRIB2 (show TRIB2 Proteins)-mediated degradation of CDC25C is associated with lysine-48-linked CDC25C polyubiquitination driven by the TRIB2 (show TRIB2 Proteins) kinase-like domain.
the biology of the activation/deactivation of CDC25 (show RASGRF1 Proteins) by kinases/phosphatases to maintain the level of CDK (show CDK4 Proteins)-cyclin (show PCNA Proteins) activities and thus the genomic stability
the knockdown of CDC25C can reduce both the radiotherapy sensitivity and the proliferation activity of EC9706 cells.
results identify CDC25C as a downstream target of the mutated tyrosine kinase (show TXK Proteins) FLT3 (show FLT3 Proteins)-ITD affecting cell-cycle regulation in a model of AML (show RUNX1 Proteins)
Suggest that the p53-p21-DREAM-CDE/CHR pathway regulates p53-dependent repression of Survivin, CDC25C, and PLK1 in HCT116 cells.
Data indicate that nine compounds were identified with Ki values for CDC25A, -B and -C ranging from 0.01 to 4.4 muM.
These miR (show MLXIP Proteins)-142-3p functioned as a tumor suppressor by targeting CDC25C.
Cdc25C negatively regulates proapoptotic ASK1 (show MAP3K5 Proteins) in a cell cycle-dependent manner and may play a role in G2/M checkpoint-mediated apoptosis.
oxidative stress-induced (show SQSTM1 Proteins) DNA damage of mouse zygotes triggers the cell cycle checkpoint, which results in G2/M cell cycle arrest, and that phospho-Cdc25B (show CDC25B Proteins) (Ser323), phospho-Cdc25C (Ser216), and phospho-Cdc2 (show CDK1 Proteins) (Tyr15) participate in activating the G2/M checkpoint.
The role of Cdc25c and Cdc25b (show CDC25B Proteins) in activating G2/M cell cycle checkpoint in zygote.
an asymmetrical distribution pattern for Cdc25c transcripts in 2-cell embryos.
CDC25A (show CDC25A Proteins) and CDC25B (show CDC25B Proteins) but not CDC25C compensate for each other to maintain the proliferative capacity of intestinal epithelial stem and progenitor cells
A single cell cycle genes homology region controls transcription of the cdc25C gene and is able to cooperate with E2F (show E2F1 Proteins) or Sp1 (show SP1 Proteins)/3 sites
Cdc25A (show CDC25A Proteins), or possibly other phosphatases, is able to functionally compensate for the loss of Cdc25B (show CDC25B Proteins) and Cdc25C in mice
The present study was aimed to investigate the possibility that selenium (Se)-induced oxidative stress mediated alterations in Cdc25c and p21 may cause modulations in the CDC2 (show CDK1 Proteins)/Cyclin B1 (show CCNB1 Proteins) complex responsible for G2/M phase checkpoint in spermatogenesis.
In Lzts1 (show LZTS1 Proteins)(-/-) mouse embryo fibroblasts (MEFs), Cdc25C degradation was increased during M phase, resulting in decreased Cdk1 (show CDK1 Proteins) activity.
PP2A:B56delta as a key upstream regulator of Cdk1 (show CDK1 Proteins) activity upon exit from mitosis
Blocking mitotic entry by adding the catalytic subunit of protein kinase A results in increased wee1 Ser549 phosphorylation and maintenance of cdc25C.
These observations identify PP2A (show PPP2R2B Proteins)/B56delta as a central checkpoint effector and suggest a mechanism for controlling 14-3-3 (show YWHAQ Proteins) interactions to promote mitosis.
In Xenopus oocytes, p42 MAPK (show MAPK1 Proteins) interacts with hypophosphorylated Cdc25 before meiotic induction. During meiotic induction, p42 MAPK (show MAPK1 Proteins) phosphorylates Cdc25 at three sites, increasing Cdc25's phosphatase activity.
This gene is highly conserved during evolution and it plays a key role in the regulation of cell division. The encoded protein is a tyrosine phosphatase and belongs to the Cdc25 phosphatase family. It directs dephosphorylation of cyclin B-bound CDC2 and triggers entry into mitosis. It is also thought to suppress p53-induced growth arrest. Multiple alternatively spliced transcript variants of this gene have been described, however, the full-length nature of many of them is not known.
cell division cycle 25 homolog C (S. pombe)
, m-phase inducer phosphatase 3-like
, cell division cycle 25 homolog C
, cell division cycle 25C
, Dual specificity phosphatase Cdc25C
, M-phase inducer phosphatase 3
, dual specificity phosphatase Cdc25C
, dual specificity phosphatase CDC25C
, mitosis inducer CDC25
, phosphotyrosine phosphatase
, protein phosphatase 1, regulatory subunit 60
, cell cycle phosphatase CDC25C
, cell division cycle control protein 25C