CDC25A

From Wikipedia, the free encyclopedia

Cell division cycle 25 homolog A (S. pombe)

PDB rendering based on 1c25.

Available structures: 1c25

Identifiers

Symbol(s)

CDC25A; CDC25A2

External IDs

OMIM: 116947 MGI: 103198 HomoloGene: 1355

Gene ontology
Molecular Function:	• protein tyrosine phosphatase activity • hydrolase activity
Cellular Component:	• cellular_component • intracellular
Biological Process:	• regulation of cyclin-dependent protein kinase activity • protein amino acid dephosphorylation • cell cycle • mitosis • cell proliferation • cell division

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001789 (mRNA)
NP_001780 (protein)

NM_007658 (mRNA)
NP_031684 (protein)

Location

Chr 3: 48.17 - 48.2 Mb

Chr 9: 109.73 - 109.75 Mb

Pubmed search

[1]

[2]

Cell division cycle 25 homolog A (S. pombe), also known as CDC25A, is a human gene.

CDC25A is a member of the CDC25 family of phosphatases. CDC25A is required for progression from G1 to the S phase of the cell cycle. It activates the cyclin-dependent kinase CDC2 by removing two phosphate groups. CDC25A is specifically degraded in response to DNA damage, which prevents cells with chromosomal abnormalities from progressing through cell division. CDC25A is an oncogene, although its exact role in oncogenesis has not been demonstrated. Two transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] References

^ Entrez Gene: CDC25A cell division cycle 25 homolog A (S. pombe).

[edit] Further reading

Parsons R (1998). "Phosphatases and tumorigenesis.". Current opinion in oncology 10 (1): 88–91. PMID 9466490.
Kerkhoff E, Rapp UR (1998). "Cell cycle targets of Ras/Raf signalling.". Oncogene 17 (11 Reviews): 1457–62. doi:10.1038/sj.onc.1202185. PMID 9779991.
Nilsson I, Hoffmann I (2000). "Cell cycle regulation by the Cdc25 phosphatase family.". Progress in cell cycle research 4: 107–14. PMID 10740819.
Galaktionov K, Beach D (1992). "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins.". Cell 67 (6): 1181–94. PMID 1836978.
Conklin DS, Galaktionov K, Beach D (1995). "14-3-3 proteins associate with cdc25 phosphatases.". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7892–6. PMID 7644510.
Galaktionov K, Lee AK, Eckstein J, et al. (1995). "CDC25 phosphatases as potential human oncogenes.". Science 269 (5230): 1575–7. PMID 7667636.
Galaktionov K, Jessus C, Beach D (1995). "Raf1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation.". Genes Dev. 9 (9): 1046–58. PMID 7744247.
Demetrick DJ, Beach DH (1994). "Chromosome mapping of human CDC25A and CDC25B phosphatases.". Genomics 18 (1): 144–7. doi:10.1006/geno.1993.1440. PMID 8276402.
Xu X, Burke SP (1996). "Roles of active site residues and the NH2-terminal domain in the catalysis and substrate binding of human Cdc25.". J. Biol. Chem. 271 (9): 5118–24. PMID 8617791.
Tiefenbrun N, Melamed D, Levy N, et al. (1996). "Alpha interferon suppresses the cyclin D3 and cdc25A genes, leading to a reversible G0-like arrest.". Mol. Cell. Biol. 16 (7): 3934–44. PMID 8668211.
Huang TS, Shu CH, Yang WK, Whang-Peng J (1997). "Activation of CDC 25 phosphatase and CDC 2 kinase involved in GL331-induced apoptosis.". Cancer Res. 57 (14): 2974–8. PMID 9230211.
Fauman EB, Cogswell JP, Lovejoy B, et al. (1998). "Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A.". Cell 93 (4): 617–25. PMID 9604936.
Coqueret O, Bérubé G, Nepveu A (1998). "The mammalian Cut homeodomain protein functions as a cell-cycle-dependent transcriptional repressor which downmodulates p21WAF1/CIP1/SDI1 in S phase.". EMBO J. 17 (16): 4680–94. doi:10.1093/emboj/17.16.4680. PMID 9707427.
Iavarone A, Massagué J (1999). "E2F and histone deacetylase mediate transforming growth factor beta repression of cdc25A during keratinocyte cell cycle arrest.". Mol. Cell. Biol. 19 (1): 916–22. PMID 9858615.
Sexl V, Diehl JA, Sherr CJ, et al. (1999). "A rate limiting function of cdc25A for S phase entry inversely correlates with tyrosine dephosphorylation of Cdk2.". Oncogene 18 (3): 573–82. doi:10.1038/sj.onc.1202362. PMID 9989807.
Mochizuki T, Kitanaka C, Noguchi K, et al. (1999). "Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway.". J. Biol. Chem. 274 (26): 18659–66. PMID 10373478.
Xia K, Lee RS, Narsimhan RP, et al. (1999). "Tyrosine phosphorylation of the proto-oncoprotein Raf-1 is regulated by Raf-1 itself and the phosphatase Cdc25A.". Mol. Cell. Biol. 19 (7): 4819–24. PMID 10373531.
Vigo E, Müller H, Prosperini E, et al. (1999). "CDC25A phosphatase is a target of E2F and is required for efficient E2F-induced S phase.". Mol. Cell. Biol. 19 (9): 6379–95. PMID 10454584.