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  • Wee1
  • However, it has been difficult to clearly demonstrate that Wee1 and Cdc25 play a direct role in the control of cell growth because mutants may indirectly cause cell size defects by allowing more or less time to grow. (rupress.org)
  • A full understanding of Cdk1 inhibitory phosphorylation will require elucidation of the mechanisms that regulate Wee1 and Cdc25. (rupress.org)
  • Thus, CDK1 forms a positive feedback loop with Cdc25 and a double negative feedback loop with Wee1 (essentially a net positive feedback loop). (wikipedia.org)
  • Wee1, conserved among all eukaryotes phosphorylates Tyr15, whereas members of the Cdc25 family are phosphatases, counteracting this activity. (wikipedia.org)
  • Absence of cdc25 arrests cells in G2, but still allows activation of the G2-M checkpoint, implicating activation of wee1 and deactivation of cdc25 as important regulatory steps in the checkpoint. (wikipedia.org)
  • An increasingly stable wee1 further inhibits cdc2 activity, while an inactive cdc25 prevents removal of this inhibition, resulting in a strong G2 arrest. (wikipedia.org)
  • A balance of Wee1 and Cdc25 activity with changes in cell size is coordinated by the mitotic entry control system. (wikipedia.org)
  • inhibitors
  • A large number of potent small-molecule Cdc25 Inhibitors have been identified that bind to the active site and belong to various chemical classes, including natural products, lipophilic acids, quinonoids, electrophiles, sulfonylated aminothiazoles and phosphate bioisosteres. (wikipedia.org)
  • budding yeast
  • To learn more about the mechanisms that regulate entry into mitosis, we have characterized the function and regulation of Mih1, the budding yeast homologue of Cdc25. (rupress.org)
  • Cdk1
  • CDK1 is dephosphorylated primarily through the actions of Cdc25, which can dephosphorylate both the Thr14 and Tyr15 residues of CDK1. (wikipedia.org)
  • Active Cdk1 is also capable of phosphorylating and activating Cdc25 and thus promote its own activation, resulting in a positive feedback loop. (wikipedia.org)
  • Regulation
  • There are three isoforms of Cdc25 (A, B, and C) in mammalian cells, all of which have been shown to have roles in regulation of G2 phase. (wikipedia.org)
  • substrate
  • A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. (ebi.ac.uk)
  • Genes
  • An exception is the nematode Caenorhabditis elegans, which has four distinct Cdc25 genes (Cdc-25.1 to Cdc-25.4). (wikipedia.org)
  • family
  • The Cdc25 family appears to have expanded in relation to the complexity of the cell-cycle and life-cycle of higher animals. (wikipedia.org)
  • PMID
  • The crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), has been determined at 2.1 angstrom resolution [ PMID: 8650541 ]. (ebi.ac.uk)
  • enzymes
  • Cdc25 enzymes are well conserved through evolution, and have been isolated from fungi such as yeasts as well as all metazoans examined to date, including humans. (wikipedia.org)
  • cell cycle
  • Instead, 14-3-3 may facilitate the association of cdc25 with Raf-1 in vivo, participating in the linkage between mitogenic signaling and the cell cycle machinery. (cshl.edu)
  • This mutant, called rr31 , is a fully dominant, maternal-effect, gain-of-function mutation in the cdc-25.1 cell cycle phosphatase that sensitizes the intestinal lineage to an extra cell division. (biologists.org)
  • Cdc25 is a dual-specificity phosphatase first isolated from the yeast Schizosaccharomyces pombe as a cell cycle defective mutant. (wikipedia.org)
  • selective
  • The most potent was 6-chloro-7-(2-morpholin-4-ylethylamino)quinoline-5,8-dione (NSC 663284), which was 20- and 450-fold more selective against Cdc25B2 as compared with VHR or PTP1B phosphatases, respectively. (pitt.edu)
  • DUSPs
  • All DUSPs contain a common phosphatase domain with conserved aspartic acid, cysteine, and arginine residues forming the catalytic site. (scitechnol.com)