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Science 15 September 1995:
Vol. 269. no. 5230, pp. 1575 - 1577
DOI: 10.1126/science.7667636

Articles

Science, Vol 269, Issue 5230, 1575-1577
Copyright © 1995 by American Association for the Advancement of Science


articles

CDC25 phosphatases as potential human oncogenes

K Galaktionov, AK Lee, J Eckstein, G Draetta, J Meckler, M Loda, and D Beach

Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724, USA.

Cyclin-dependent kinases (CDKs) are activated by CDC25 phosphatases, which remove inhibitory phosphate from tyrosine and threonine residues. In human cells, CDC25 proteins are encoded by a multigene family, consisting of CDC25A, CDC25B, and CDC25C. In rodent cells, human CDC25A or CDC25B but not CDC25C phosphatases cooperate with either Ha-RASG12V or loss of RB1 in oncogenic focus formation. Such transformants were highly aneuploid, grew in soft agar, and formed high-grade tumors in nude mice. Overexpression of CDC25B was detected in 32 percent of human primary breast cancers tested. The CDC25 phosphatases may contribute to the development of human cancer.


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An Essential Phosphorylation-site Domain of Human cdc25C Interacts with Both 14-3-3 and Cyclins.
M. C. Morris, A. Heitz, J. Mery, F. Heitz, and G. Divita (2000)
J. Biol. Chem. 275, 28849-28857
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Arsenite-induced Cdc25C degradation is through the KEN-box and ubiquitin-proteasome pathway.
F. Chen, Z. Zhang, J. Bower, Y. Lu, S. S. Leonard, M. Ding, V. Castranova, H. Piwnica-Worms, and X. Shi (2002)
PNAS 99, 1990-1995
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Science. ISSN 0036-8075 (print), 1095-9203 (online)