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Journal articles on the topic 'CDC25Mm'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Ferguson, Angela M., Lynn S. White, Peter J. Donovan, and Helen Piwnica-Worms. "Normal Cell Cycle and Checkpoint Responses in Mice and Cells Lacking Cdc25B and Cdc25C Protein Phosphatases." Molecular and Cellular Biology 25, no. 7 (2005): 2853–60. http://dx.doi.org/10.1128/mcb.25.7.2853-2860.2005.

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ABSTRACT The Cdc25 family of protein phosphatases positively regulates cell division by activating cyclin-dependent protein kinases (CDKs). In humans and rodents, there are three Cdc25 family members—denoted Cdc25A, Cdc25B, and Cdc25C—that can be distinguished based on their subcellular compartmentalizations, their abundances and/or activities throughout the cell cycle, the CDKs that they target for activation, and whether they are overexpressed in human cancers. In addition, murine forms of Cdc25 exhibit distinct patterns of expression throughout development and in adult tissues. These proper

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2

Lammer, C., S. Wagerer, R. Saffrich, D. Mertens, W. Ansorge, and I. Hoffmann. "The cdc25B phosphatase is essential for the G2/M phase transition in human cells." Journal of Cell Science 111, no. 16 (1998): 2445–53. http://dx.doi.org/10.1242/jcs.111.16.2445.

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Cdc25 phosphatases play key roles in cell cycle progression by activating cyclin-dependent kinases. In human cells, cdc25 proteins are encoded by a multigene family, consisting of cdc25A, cdc25B and cdc25C. While cdc25A plays a crucial role at the G1/S phase transition, cdc25C is involved in the dephosphorylation and activation of the mitotic kinase, cdc2/cyclinB. In addition, cdc25C itself is regulated by cdc2/cyclinB which then creates a positive feedback loop that controls entry into mitosis. In this study we show that the activity of cdc25B appears during late S phase and peaks during G2 p

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3

Cen, H., A. G. Papageorge, W. C. Vass, K. E. Zhang, and D. R. Lowy. "Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor." Molecular and Cellular Biology 13, no. 12 (1993): 7718–24. http://dx.doi.org/10.1128/mcb.13.12.7718-7724.1993.

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Serum stimulates cells to increase their proportion of Ras protein in the active GTP-bound state. We have recently identified four types (I to IV) of apparently full-length cDNAs from a single mammalian gene, called CDC25Mm or GRF, which is homologous to the Ras-specific exchange factor CDC25 of S. cerevisiae. The largest cDNA (type IV) is brain specific, with the other three classes, although they have distinct 5' ends, essentially representing progressive N-terminal deletions of this cDNA. When placed in a retroviral expression vector, all four types of cDNAs induced morphologic transformati

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4

Cen, H., A. G. Papageorge, W. C. Vass, K. E. Zhang, and D. R. Lowy. "Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor." Molecular and Cellular Biology 13, no. 12 (1993): 7718–24. http://dx.doi.org/10.1128/mcb.13.12.7718.

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Serum stimulates cells to increase their proportion of Ras protein in the active GTP-bound state. We have recently identified four types (I to IV) of apparently full-length cDNAs from a single mammalian gene, called CDC25Mm or GRF, which is homologous to the Ras-specific exchange factor CDC25 of S. cerevisiae. The largest cDNA (type IV) is brain specific, with the other three classes, although they have distinct 5' ends, essentially representing progressive N-terminal deletions of this cDNA. When placed in a retroviral expression vector, all four types of cDNAs induced morphologic transformati

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5

Lindqvist, Arne, Helena Källström, Andreas Lundgren, Emad Barsoum, and Christina Karlsson Rosenthal. "Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1–Cdk1 at the centrosome." Journal of Cell Biology 171, no. 1 (2005): 35–45. http://dx.doi.org/10.1083/jcb.200503066.

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Cdc25 phosphatases are essential for the activation of mitotic cyclin–Cdks, but the precise roles of the three mammalian isoforms (A, B, and C) are unclear. Using RNA interference to reduce the expression of each Cdc25 isoform in HeLa and HEK293 cells, we observed that Cdc25A and -B are both needed for mitotic entry, whereas Cdc25C alone cannot induce mitosis. We found that the G2 delay caused by small interfering RNA to Cdc25A or -B was accompanied by reduced activities of both cyclin B1–Cdk1 and cyclin A–Cdk2 complexes and a delayed accumulation of cyclin B1 protein. Further, three-dimension

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6

Wickramasinghe, D., S. Becker, M. K. Ernst, et al. "Two CDC25 homologues are differentially expressed during mouse development." Development 121, no. 7 (1995): 2047–56. http://dx.doi.org/10.1242/dev.121.7.2047.

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The cdc25 gene product is a tyrosine phosphatase that acts as an initiator of M-phase in eukaryotic cell cycles by activating p34cdc2. Here we describe the cloning and characterization of the developmental expression pattern of two mouse cdc25 homologs. Sequence comparison of the mouse genes with human CDC25 genes reveal that they are most likely the mouse homologs of human CDC25A and CDC25B respectively. Mouse cdc25a, which has not been described previously, shares 84% sequence identity with human CDC25A and has a highly conserved phosphatase domain characteristic of all cdc25 genes. A glutat

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7

Chen, Mei-Shya, Jonathan Hurov, Lynn S. White, Terry Woodford-Thomas, and Helen Piwnica-Worms. "Absence of Apparent Phenotype in Mice Lacking Cdc25C Protein Phosphatase." Molecular and Cellular Biology 21, no. 12 (2001): 3853–61. http://dx.doi.org/10.1128/mcb.21.12.3853-3861.2001.

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ABSTRACT The Cdc25 family of protein phosphatases positively regulate the cell division cycle by activating cyclin-dependent protein kinases. In humans and rodents, three Cdc25 family members denoted Cdc25A, -B, and -C have been identified. The murine forms of Cdc25 exhibit distinct patterns of expression both during development and in adult mouse tissues. In order to determine unique contributions made by the Cdc25C protein phosphatase to embryonic and adult cell cycles, mice lacking Cdc25C were generated. We report thatCdc25C −/− mice are viable and do not display any obvious abnormalities.

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8

Zhou, Xiaokun, Danping Lu, Wenxiang Yi, and Dan Xu. "Downregulation of CDC25C in NPCs Disturbed Cortical Neurogenesis." International Journal of Molecular Sciences 24, no. 2 (2023): 1505. http://dx.doi.org/10.3390/ijms24021505.

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Cell division regulators play a vital role in neural progenitor cell (NPC) proliferation and differentiation. Cell division cycle 25C (CDC25C) is a member of the CDC25 family of phosphatases which positively regulate cell division by activating cyclin-dependent protein kinases (CDKs). However, mice with the Cdc25c gene knocked out were shown to be viable and lacked the apparent phenotype due to genetic compensation by Cdc25a and/or Cdc25b. Here, we investigate the function of Cdc25c in developing rat brains by knocking down Cdc25c in NPCs using in utero electroporation. Our results indicate th

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9

Jacquet, Eric, Soria Baouz, and Andrea Parmeggiani. "Characterization of mammalian C-CDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21.cntdot.C-CDC25Mm." Biochemistry 34, no. 38 (1995): 12347–54. http://dx.doi.org/10.1021/bi00038a031.

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10

Kang, Min, Aera Bang, Ok Choi, and Seung Han. "Comparative analysis of two murine CDC25B isoforms." Archives of Biological Sciences 69, no. 1 (2017): 35–44. http://dx.doi.org/10.2298/abs160315062k.

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CDC25B phosphatase plays a pivotal role in the cell cycle process by dephosphorylating and activating the CDC2 kinase of maturation-promoting factor (MPF). In mice, two transcripts of Cdc25B are generated by the alternative splicing of one gene. We compared the properties of these two forms of CDC25B. When the expression pattern of Cdc25B was examined using RT-PCR, both forms were detected in almost all mouse tissues tested. The expression of two forms of the CDC25B protein in various mouse tissues was confirmed using Western blotting with generated isoform specific antibodies. CDC25B1 tends t

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11

Nishijima, Hitoshi, Hideo Nishitani, Takashi Seki, and Takeharu Nishimoto. "A Dual-Specificity Phosphatase Cdc25B Is an Unstable Protein and Triggers p34cdc2/Cyclin B Activation in Hamster BHK21 Cells Arrested with Hydroxyurea." Journal of Cell Biology 138, no. 5 (1997): 1105–16. http://dx.doi.org/10.1083/jcb.138.5.1105.

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By incubating at 30°C in the presence of an energy source, p34cdc2/cyclin B was activated in the extract prepared from a temperature-sensitive mutant, tsBN2, which prematurely enters mitosis at 40°C, the nonpermissive temperature (Nishimoto, T., E. Eilen, and C. Basilico. 1978. Cell. 15:475–483), and wild-type cells of the hamster BHK21 cell line arrested in S phase, without protein synthesis. Such an in vitro activation of p34cdc2/cyclin B, however, did not occur in the extract prepared from cells pretreated with protein synthesis inhibitor cycloheximide, although this extract still retained

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12

Blomberg, Ida, and Ingrid Hoffmann. "Ectopic Expression of Cdc25A Accelerates the G1/S Transition and Leads to Premature Activation of Cyclin E- and Cyclin A-Dependent Kinases." Molecular and Cellular Biology 19, no. 9 (1999): 6183–94. http://dx.doi.org/10.1128/mcb.19.9.6183.

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ABSTRACT Human Cdc25 phosphatases play important roles in cell cycle regulation by removing inhibitory phosphates from tyrosine and threonine residues of cyclin-dependent kinases. Three human Cdc25 isoforms, A, B, and C, have been discovered. Cdc25B and Cdc25C play crucial roles at the G2/M transition. In the present study, we have investigated the function of human Cdc25A phosphatase. Cell lines that express human Cdc25A in an inducible manner have been generated. Ectopic expression of Cdc25A accelerates the G1/S-phase transition, indicating that Cdc25A controls an event(s) that is rate limit

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13

Innocenti, Metello, Renata Zippel, Riccardo Brambilla, and Emmapaola Sturani. "CDC25Mm /Ras-GRF1 regulates both Ras and Rac signaling pathways." FEBS Letters 460, no. 2 (1999): 357–62. http://dx.doi.org/10.1016/s0014-5793(99)01374-5.

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14

Turowski, Patric, Celine Franckhauser, May C. Morris, Philippe Vaglio, Anne Fernandez, and Ned J. C. Lamb. "Functional cdc25C Dual-Specificity Phosphatase Is Required for S-Phase Entry in Human Cells." Molecular Biology of the Cell 14, no. 7 (2003): 2984–98. http://dx.doi.org/10.1091/mbc.e02-08-0515.

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In view of the common regulatory mechanism that induces transcription of the mitotic phosphatase cdc25C and cyclin A at the beginning of S-phase, we investigated whether cdc25C was required for S-phase transit. Here, we show that in both nontransformed human fibroblasts and HeLa cells, cdc25C protein levels significantly increased concomitant with S-phase onset and cyclin A synthesis. Activity measurements on immunoprecipitates from synchronized HeLa cells revealed a sharp rise in cdc25C-associated phosphatase activity that coincided with S-phase. Microinjection of various antisense-cdc25C mol

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15

Mattingly, Raymond R., Vijay Saini, and Ian G. Macara. "Activation of the Ras-GRF/CDC25Mm Exchange Factor by Lysophosphatidic Acid." Cellular Signalling 11, no. 8 (1999): 603–10. http://dx.doi.org/10.1016/s0898-6568(99)00034-0.

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16

Coccetti, P., I. Mauri, L. Alberghina, E. Martegani, and A. Parmeggiani. "The Minimal Active Domain of the Mouse Ras Exchange Factor CDC25Mm." Biochemical and Biophysical Research Communications 206, no. 1 (1995): 253–59. http://dx.doi.org/10.1006/bbrc.1995.1035.

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17

Kiyono, M., T. Satoh, and Y. Kaziro. "G protein subunit-dependent Rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25Mm." Proceedings of the National Academy of Sciences 96, no. 9 (1999): 4826–31. http://dx.doi.org/10.1073/pnas.96.9.4826.

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18

Tonini, Raffaella, Silvana Franceschetti, Daniela Parolaro, et al. "Involvement of CDC25Mm/Ras-GRF1-Dependent Signaling in the Control of Neuronal Excitability." Molecular and Cellular Neuroscience 18, no. 6 (2001): 691–701. http://dx.doi.org/10.1006/mcne.2001.1050.

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19

Sturani, Emmapaola, Adele Abbondio, Paola Branduardi, et al. "The Ras Guanine Nucleotide Exchange Factor CDC25Mm Is Present at the Synaptic Junction." Experimental Cell Research 235, no. 1 (1997): 117–23. http://dx.doi.org/10.1006/excr.1997.3660.

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20

Coccetti, Paola, Enrico Monzani, Lilia Alberghina, Luigi Casella, and Enzo Martegani. "Analysis of the secondary structure of the catalytic domain of mouse Ras exchange factor CDC25Mm." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1383, no. 2 (1998): 292–300. http://dx.doi.org/10.1016/s0167-4838(97)00212-4.

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21

Karlsson, Christina, Stephanie Katich, Anja Hagting, Ingrid Hoffmann, and Jonathon Pines. "Cdc25b and Cdc25c Differ Markedly in Their Properties as Initiators of Mitosis." Journal of Cell Biology 146, no. 3 (1999): 573–84. http://dx.doi.org/10.1083/jcb.146.3.573.

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We have used time-lapse fluorescence microscopy to study the properties of the Cdc25B and Cdc25C phosphatases that have both been implicated as initiators of mitosis in human cells. To differentiate between the functions of the two proteins, we have microinjected expression constructs encoding Cdc25B or Cdc25C or their GFP-chimeras into synchronized tissue culture cells. This assay allows us to express the proteins at defined points in the cell cycle. We have followed the microinjected cells by time-lapse microscopy, in the presence or absence of DNA synthesis inhibitors, and assayed whether t

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22

Consonni, Roberto, Ivana Arosio, Teresa Recca, Renato Longhi, Giorgio Colombo, and Marco Vanoni. "Structure Determination and Dynamics of Peptides Overlapping the Catalytic Hairpin of the Ras-Specific GEF Cdc25Mm†." Biochemistry 42, no. 42 (2003): 12154–62. http://dx.doi.org/10.1021/bi0344026.

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23

Vanoni, Marco, Riccardo Bertini, Elena Sacco, et al. "Characterization and Properties of Dominant-negative Mutants of the Ras-specific Guanine Nucleotide Exchange Factor CDC25Mm." Journal of Biological Chemistry 274, no. 51 (1999): 36656–62. http://dx.doi.org/10.1074/jbc.274.51.36656.

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24

Ferrari, C., R. Zippel, E. Martegani, N. Gnesutta, V. Carrera, and E. Sturani. "Expression of Two Different Products of CDC25Mm, a Mammalian Ras Activator, during Development of Mouse Brain." Experimental Cell Research 210, no. 2 (1994): 353–57. http://dx.doi.org/10.1006/excr.1994.1048.

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25

Baouz, Soria, Eric Jacquet, Katia Accorsi, et al. "Sites of Phosphorylation by Protein Kinase A in CDC25Mm/GRF1, a Guanine Nucleotide Exchange Factor for Ras." Journal of Biological Chemistry 276, no. 3 (2000): 1742–49. http://dx.doi.org/10.1074/jbc.m005770200.

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26

Gariboldi, Manuela, Emmapaola Sturani, Federico Canzian, et al. "Genetic Mapping of the Mouse CDC25Mm Gene, a Ras-Specific Guanine Nucleotide-Releasing Factor, to Chromosome 9." Genomics 21, no. 2 (1994): 451–53. http://dx.doi.org/10.1006/geno.1994.1295.

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27

List, Alan F., Kathy Rocha, Ling Zhang, et al. "Secondary Resistance to Lenalidomide in Del(5q) MDS Is Associated with CDC25C & PP2A Overexpression." Blood 114, no. 22 (2009): 292. http://dx.doi.org/10.1182/blood.v114.22.292.292.

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Abstract Abstract 292 Background: Allelic deficiency for the RPS14 gene impairs differentiation and survival of erythroid progenitors in del(5q) MDS (Nature 2008; 451:335). Nucleolar stress arising from disruption of ribosome assembly fosters MDM2 sequestration by free ribosome components resulting in p53 stabilization and erythroid hypoplasia (Nat Cell Biol 2009; 11:501). We recently reported that reduced gene dosage of the lenalidomide (LEN) inhibitable, haplodeficient phosphatases CDC25C and PP2Acα is a key determinant of drug sensitivity in del(5q) MDS (PNAS 2009; 106: 12974). We now show

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28

Lee, M. S., S. Ogg, M. Xu, et al. "cdc25+ encodes a protein phosphatase that dephosphorylates p34cdc2." Molecular Biology of the Cell 3, no. 1 (1992): 73–84. http://dx.doi.org/10.1091/mbc.3.1.73.

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To determine how the human cdc25 gene product acts to regulate p34cdc2 at the G2 to M transition, we have overproduced the full-length protein (cdc25Hs) as well as several deletion mutants in bacteria as glutathione-S-transferase fusion proteins. The wild-type cdc25Hs gene product was synthesized as an 80-kDa fusion protein (p80GST-cdc25) and was judged to be functional by several criteria: recombinant p80GST-cdc25 induced meiotic maturation of Xenopus oocytes in the presence of cycloheximide; p80GST-cdc25 activated histone H1 kinase activity upon addition to extracts prepared from Xenopus ooc

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29

Gabrielli, B. G., C. P. De Souza, I. D. Tonks, J. M. Clark, N. K. Hayward, and K. A. Ellem. "Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells." Journal of Cell Science 109, no. 5 (1996): 1081–93. http://dx.doi.org/10.1242/jcs.109.5.1081.

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The formation of the mitotic spindle is an essential prerequisite for successful mitosis. The dramatic changes in the level of microtubule (Mt) nucleation at the centrosomes and Mt dynamics that occur in prophase are presumed to be initiated through the activity of cdc2/cyclin B. Here we present data that the cdc25B isoform functions to activate the cytoplasmic pool of cdc2/cyclin B responsible for these events. In contrast to cdc25C, cdc25B is present at low levels in HeLa cells during interphase, but sharply increases in prophase, when cdc25B accumulation in the cytoplasm correlates with pro

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30

Mattingly, Raymond R., та Ian G. Macara. "Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G-protein βγ subunits". Nature 382, № 6588 (1996): 268–72. http://dx.doi.org/10.1038/382268a0.

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31

Jones, S., M. L. Vignais, and J. R. Broach. "The CDC25 protein of Saccharomyces cerevisiae promotes exchange of guanine nucleotides bound to ras." Molecular and Cellular Biology 11, no. 5 (1991): 2641–46. http://dx.doi.org/10.1128/mcb.11.5.2641-2646.1991.

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The product of the CDC25 gene of Saccharomyces cerevisiae, in its capacity as an activator of the RAS/cyclic AMP pathway, is required for initiation of the cell cycle. In this report, we provide an identification of Cdc25p, the product of the CDC25 gene, and evidence that it promotes exchange of guanine nucleotides bound to Ras in vitro. Extracts of strains containing high levels of Cdc25p catalyze both removal of GDP from and the concurrent binding of GTP to Ras. This same activity is also obtained with an immunopurified Cdc25p-beta-galactosidase fusion protein, suggesting that Cdc25p partici

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32

Jones, S., M. L. Vignais, and J. R. Broach. "The CDC25 protein of Saccharomyces cerevisiae promotes exchange of guanine nucleotides bound to ras." Molecular and Cellular Biology 11, no. 5 (1991): 2641–46. http://dx.doi.org/10.1128/mcb.11.5.2641.

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The product of the CDC25 gene of Saccharomyces cerevisiae, in its capacity as an activator of the RAS/cyclic AMP pathway, is required for initiation of the cell cycle. In this report, we provide an identification of Cdc25p, the product of the CDC25 gene, and evidence that it promotes exchange of guanine nucleotides bound to Ras in vitro. Extracts of strains containing high levels of Cdc25p catalyze both removal of GDP from and the concurrent binding of GTP to Ras. This same activity is also obtained with an immunopurified Cdc25p-beta-galactosidase fusion protein, suggesting that Cdc25p partici

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33

Lenzen, Christian, Robbert H. Cool, Heino Prinz, Jürgen Kuhlmann, and Alfred Wittinghofer. "Kinetic Analysis by Fluorescence of the Interaction between Ras and the Catalytic Domain of the Guanine Nucleotide Exchange Factor Cdc25Mm †." Biochemistry 37, no. 20 (1998): 7420–30. http://dx.doi.org/10.1021/bi972621j.

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34

Giglione, Carmela, Stefania Gonfloni, and Andrea Parmeggiani. "Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm." European Journal of Biochemistry 268, no. 11 (2001): 3275–83. http://dx.doi.org/10.1046/j.1432-1327.2001.02230.x.

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35

Baouz, Soria, Eric Jacquet, Alberto Bernardi, and Andrea Parmeggiani. "The N-terminal Moiety of CDC25Mm, a GDP/GTP Exchange Factor of Ras Proteins, Controls the Activity of the Catalytic Domain." Journal of Biological Chemistry 272, no. 10 (1997): 6671–76. http://dx.doi.org/10.1074/jbc.272.10.6671.

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36

Gnesutta, Nerina, Michela Ceriani, Metello Innocenti, et al. "Cloning and Characterization of Mouse UBPy, a Deubiquitinating Enzyme That Interacts with the Ras Guanine Nucleotide Exchange Factor CDC25Mm/Ras-GRF1." Journal of Biological Chemistry 276, no. 42 (2001): 39448–54. http://dx.doi.org/10.1074/jbc.m103454200.

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Gershon, Eran, Dalia Galiani, and Nava Dekel. "Cytoplasmic polyadenylation controls cdc25B mRNA translation in rat oocytes resuming meiosis." Reproduction 132, no. 1 (2006): 21–31. http://dx.doi.org/10.1530/rep.1.01093.

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Resumption of meiosis in oocytes represents the entry into M-phase of the cell cycle and is regulated by the maturation-promoting factor (MPF). Activation of MPF is catalyzed by the dual specificity phosphatase, cdc25. In mammals, cdc25 is represented by a multigene family consisting of three isoforms: A, B and C. A recent report that female mice lacking cdc25B exhibit impaired fertility suggests a role for this isoform in regulating the G2- to M-transition in mammalian oocytes. Supporting the above-mentioned observation, we demonstrate herein that microinjection of neutralizing antibodies aga

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Li, Qianyi, Haoran Jin, and Shifeng Zhao. "Principles, Processes and Modalities of Interaction Between Proto-Oncoprotein PIM-1 Kinase and Cell Division Cyclin CDC25A." Highlights in Science, Engineering and Technology 45 (April 18, 2023): 176–82. http://dx.doi.org/10.54097/hset.v45i.7363.

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All malignant tumors with aberrant cell differentiation and proliferation, unchecked growth, invasion, and metastasis are referred to as cancer. Its occurrence is a multi-step, complex process with many contributing components. Proto oncoprotein and The PIM kinase family is crucial to this procedure., and proto oncoprotein PIM-1 kinase is an important member of PIM family. The expression of proto oncoprotein PIM-1 is positively correlated with the status of lymphatic metastasis, and its overexpression could promote cell cycle and inhibit apoptosis. Cell division cycle 25 (CDC25) is a bispecifi

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39

Hernández, Silvia, Luis Hernández, Sílvia Bea, et al. "cdc25a and the splicing variant cdc25b2, but not cdc25B1, -B3 or -C, are over-expressed in aggressive human non-Hodgkin's lymphomas." International Journal of Cancer 89, no. 2 (2000): 148–52. http://dx.doi.org/10.1002/(sici)1097-0215(20000320)89:2<148::aid-ijc8>3.0.co;2-r.

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40

Demetrick, Douglas J., and David H. Beach. "Chromosome Mapping of Human CDC25A and CDC25B Phosphatases." Genomics 18, no. 1 (1993): 144–47. http://dx.doi.org/10.1006/geno.1993.1440.

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41

Shreeram, Sathyavageeswaran, Weng Kee Hee, and Dmitry V. Bulavin. "Cdc25A Serine 123 Phosphorylation Couples Centrosome Duplication with DNA Replication and Regulates Tumorigenesis." Molecular and Cellular Biology 28, no. 24 (2008): 7442–50. http://dx.doi.org/10.1128/mcb.00138-08.

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ABSTRACT The cell division cycle 25A (Cdc25A) phosphatase is a critical regulator of cell cycle progression under normal conditions and after stress. Stress-induced degradation of Cdc25A has been proposed as a major way of delaying cell cycle progression. In vitro studies pointed toward serine 123 as a key site in regulation of Cdc25A stability after exposure to ionizing radiation (IR). To address the role of this phosphorylation site in vivo, we generated a knock-in mouse in which alanine was substituted for serine 123. The Cdc25 S123A knock-in mice appeared normal, and, unexpectedly, cells d

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42

Boy-Marcotte, E., P. Ikonomi, and M. Jacquet. "SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation." Molecular Biology of the Cell 7, no. 4 (1996): 529–39. http://dx.doi.org/10.1091/mbc.7.4.529.

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The SDC25 gene of Saccharomyces cerevisiae is homologous to CDC25. Its 3' domain encodes a guanine nucleotide exchange factor (GEF) for Ras. Nevertheless, the GEF encoded by CDC24 is determinant for the Ras/cAMP pathway activation in growth. We demonstrate that the SDC25 gene product is a functional GEF for Ras: the complete SDC25 gene functionally replaces CDC25 when overexpressed or when transcribed under CDC25 transcriptional control at the CDC25 locus. Chimeric proteins between Sdc25p and Cdc25p are also functional GEFs for Ras. We also show that the two genes are differentially regulated:

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43

Ito, Y., H. Yoshida, K. Nakano, et al. "Expression of cdc25A and cdc25B proteins in thyroid neoplasms." British Journal of Cancer 86, no. 12 (2002): 1909–13. http://dx.doi.org/10.1038/sj.bjc.6600364.

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Ito, Yasuhiro, Hiroshi Yoshida, Takashi Uruno, et al. "Expression of cdc25A and cdc25B phosphatase in breast carcinoma." Breast Cancer 11, no. 3 (2004): 295–300. http://dx.doi.org/10.1007/bf02984552.

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Fernandez-Vidal, Anne, Anne Mazars, and Stephane Manenti. "CDC25A: A Rebel Within the CDC25 Phosphatases Family?" Anti-Cancer Agents in Medicinal Chemistry 8, no. 8 (2008): 825–31. http://dx.doi.org/10.2174/187152008786847684.

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Margolis, Seth S., Jennifer A. Perry, Douglas H. Weitzel, et al. "A Role for PP1 in the Cdc2/Cyclin B–mediated Positive Feedback Activation of Cdc25." Molecular Biology of the Cell 17, no. 4 (2006): 1779–89. http://dx.doi.org/10.1091/mbc.e05-08-0751.

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The Cdc25 phosphatase promotes entry into mitosis through the removal of inhibitory phosphorylations on the Cdc2 subunit of the Cdc2/CyclinB complex. During interphase, or after DNA damage, Cdc25 is suppressed by phosphorylation at Ser287 (Xenopus numbering; Ser216 of human Cdc25C) and subsequent binding of the small acidic protein, 14-3-3. As reported recently, at the time of mitotic entry, 14-3-3 protein is removed from Cdc25 and S287 is dephosphorylated by protein phosphatase 1 (PP1). After the initial activation of Cdc25 and consequent derepression of Cdc2/CyclinB, Cdc25 is further activat

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Carrera, Vittorio, Andrea Moroni, Enzo Martegani, et al. "Mutations at position 1122 in the catalytic domain of the mouse ras-specific guanine nucleotide exchange factor CDC25Mm originate both loss-of-function and gain-of-function proteins." FEBS Letters 440, no. 3 (1998): 291–96. http://dx.doi.org/10.1016/s0014-5793(98)01481-1.

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Izumi, T., and J. L. Maller. "Phosphorylation and activation of the Xenopus Cdc25 phosphatase in the absence of Cdc2 and Cdk2 kinase activity." Molecular Biology of the Cell 6, no. 2 (1995): 215–26. http://dx.doi.org/10.1091/mbc.6.2.215.

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The M-phase inducer, Cdc25C, is a dual-specificity phosphatase that directly phosphorylates and activates the cyclin B/Cdc2 kinase complex, leading to initiation of mitosis. Cdc25 itself is activated at the G2/M transition by phosphorylation on serine and threonine residues. Previously, it was demonstrated that Cdc2 kinase is capable of phosphorylating and activating Cdc25, suggesting the existence of a positive feedback loop. In the present study, kinases other than Cdc2 that can phosphorylate and activate Cdc25 were investigated. Cdc25 was found to be phosphorylated and activated by cyclin A

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Folch-Mallol, Jorge Luis, Luz María Martínez, Sergio J. Casas, et al. "New roles for CDC25 in growth control, galactose regulation and cellular differentiation in Saccharomyces cerevisiae." Microbiology 150, no. 9 (2004): 2865–79. http://dx.doi.org/10.1099/mic.0.27144-0.

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Living organisms display large differences in stress resistance throughout their life cycles. To study the coordinated regulation of development and stress responses in exponentially growing yeast, mutants that displayed elevated heat-shock resistance at this stage were screened for. Here, two new mutant alleles of CDC25 in Saccharomyces cerevisiae, cdc25-21 and cdc25-22, are described. During exponential growth in glucose at 25 °C, these mutants are resistant to heat, oxidative, osmotic and ionic shock, accumulate stress-protein transcripts, show slow growth rates, thick cell walls and glycog

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Ito, Yasuhiro, Hiroshi Yoshida, Chisato Tomoda, et al. "Expression of cdc25B and cdc25A in medullary thyroid carcinoma: cdc25B expression level predicts a poor prognosis." Cancer Letters 229, no. 2 (2005): 291–97. http://dx.doi.org/10.1016/j.canlet.2005.06.040.

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