Allosteric Wip1 phosphatase inhibition through flap-subdomain interaction

Nature Chemical Biology

Volumn 10, Issue 3, 2014, Pages 181-187

  Gilmartin, Aidan G ^a   Faitg, Thomas H ^a   Richter, Mark ^a   Groy, Arthur ^a   Seefeld, Mark A ^a   Darcy, Michael G ^a   Peng, Xin ^a   Federowicz, Kelly ^a   Yang, Jingsong ^a   Zhang, Shu Yun ^a   Minthorn, Elisabeth ^a   Jaworski, Jon Paul ^a   Schaber, Michael ^a   Martens, Stan ^a   McNulty, Dean E ^a   Sinnamon, Robert H ^a   Zhang, Hong ^a   Kirkpatrick, Robert B ^a   Nevins, Neysa ^a   Cui, Guanglei ^a   Pietrak, Beth ^a   Diaz, Elsie ^a   Jones, Amber ^a   Brandt, Martin ^a   Schwartz, Benjamin ^a   Heerding, Dirk A ^a   Kumar, Rakesh ^a   more..

^a GLAXOSMITHKLINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADMINISTRATION, ORAL; ALLOSTERIC REGULATION; AMINO ACID MOTIFS; AMINOPYRIDINES; ANIMALS; ANTINEOPLASTIC AGENTS; CATALYTIC DOMAIN; CELL LINE, TUMOR; DIPEPTIDES; DISEASE MODELS, ANIMAL; DRUG SCREENING ASSAYS, ANTITUMOR; ENZYME ACTIVATION; ENZYME INHIBITORS; FEMALE; HETEROGRAFTS; HUMANS; MICE; MICE, SCID; MODELS, BIOLOGICAL; NEOPLASMS; PHOSPHOPROTEIN PHOSPHATASES;

EID: 84894080663     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1427     Document Type: Article

References (33)

1. Lu X. et al. The type 2C phosphatase Wip1: An oncogenic regulator of tumor suppressor and DNA damage response pathways. Cancer Metastasis Rev. 27 123-135 (2008).
2. Lowe J. et al. Regulation of the Wip1 phosphatase and its effects on the stress response. Front. Biosci. 17 1480-1498 (2012).
3. Zhu Y.H. & Bulavin D.V. Wip1-Dependent Signaling Pathways in Health and Diseases in Progress in Molecular Biology and Translational Science Protein Phosphorylation in Health and Disease (ed. Shirish S.) 307-325 (Academic Press 2012).
4. Fiscella M. et al. Wip1 a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner. Proc. Natl. Acad. Sci. USA 94 6048-6053 (1997). (Pubitemid 27270633)
5. Yamaguchi H. et al. Substrate specificity of the human protein phosphatase 2Cd Wip1. Biochemistry 44 5285-5294 (2005). (Pubitemid 40489968)
6. Yamaguchi H. Durell S.R. Chatterjee D.K. Anderson C.W. & Appella E. The Wip1 phosphatase PPM1D dephosphorylates SQ/TQ motifs in checkpoint substrates phosphorylated by PI3K-like kinases. Biochemistry 46 12594-12603 (2007).
7. Schito M.L. Demidov O.N. Saito S. Ashwell J.D. & Appella E. Wip1 phosphatase-deficient mice exhibit defective T cell maturation due to sustained p53 activation. J. Immunol. 176 4818-4825 (2006).
8. Choi J. et al. Mice deficient for the wild-type p53-induced phosphatase gene (Wipl) exhibit defects in reproductive organs immune function and cell cycle control. Mol. Cell Biol. 22 1094-1105 (2002).
9. Castellino R.C. et al. Medulloblastomas overexpress the p53-inactivating oncogene WIP1/PPM1D. J. Neurooncol. 86 245-256 (2008).
10. Fuku T. Semba S. Yutori H. & Yokozaki H. Increased wild-type p53-induced phosphatase 1 (Wip1 or PPM1D) expression correlated with downregulation of checkpoint kinase 2 in human gastric carcinoma. Pathol. Int. 57 566-571 (2007). (Pubitemid 47222705)
11. Hirasawa A. et al. Association of 17q21-q24 gain in ovarian clear cell adenocarcinomas with poor prognosis and identification of PPM1D and APPBP2 as likely amplification targets. Clin. Cancer Res. 9 1995-2004 (2003).
12. Li J. et al. Oncogenic properties of PPM1D located within a breast cancer amplification epicenter at 17q23. Nat. Genet. 31 133-134 (2002).
13. Hu X. et al. Genetic alterations and oncogenic pathways associated with breast cancer subtypes. Mol. Cancer Res. 7 511-522 (2009).
14. Rauta J. et al. The serine-threonine protein phosphatase PPM1D is frequently activated through amplification in aggressive primary breast tumours. Breast Cancer Res. Treat. 95 257-263 (2006).
15. Natrajan R. et al. Tiling path genomic profiling of grade 3 invasive ductal breast cancers. Clin. Cancer Res. 15 2711-2722 (2009).
16. Saito-Ohara F. et al. PPM1D is a potential target for 17q gain in neuroblastoma. Cancer Res. 63 1876-1883 (2003).
17. Tan D.S.P. et al. PPM1D is a potential therapeutic target in ovarian clear cell carcinomas. Clin. Cancer Res. 15 2269-2280 (2009).
18. Bulavin D.V. et al. Amplification of PPM1D in human tumors abrogates p53 tumor-suppressor activity. Nat. Genet. 31 210-215 (2002).
19. Demidov O.N. et al. The role of the MKK6/p38 MAPK pathway in Wip1-dependent regulation of ErbB2-driven mammary gland tumorigenesis. Oncogene 26 2502-2506 (2007). (Pubitemid 46597262)
20. Lambros M.B. et al. PPM1D gene amplification and overexpression in breast cancer: A qRT-PCR and chromogenic in situ hybridization study. Mod. Pathol. 23 1334-1345 (2010).
21. Satoh N. et al. Oncogenic phosphatase Wip1 is a novel prognostic marker for lung adenocarcinoma patient survival. Cancer Sci. 102 1101-1106 (2011).
22. Vintonyak V.V. Antonchick A.P. Rauh D. & Waldmann H. The therapeutic potential of phosphatase inhibitors. Curr. Opin. Chem. Biol. 13 272-283 (2009).
23. Clark M.A. et al. Design synthesis and selection of DNA-encoded small-molecule libraries. Nat. Chem. Biol. 5 647-654 (2009).
24. Yamaguchi H. et al. Development of a substrate-based cyclic phosphopeptide inhibitor of protein phosphatase 2Cd Wip1. Biochemistry 45 13193-13202 (2006).
25. Chuman Y. et al. Characterization of the active site and a unique uncompetitive inhibitor of the PPM1-type protein phosphatase PPM1D. Protein Pept. Lett. 15 938-948 (2008).
26. Pullen K.E. et al. An alternate conformation and a third metal in PstP/Ppp the M. tuberculosis PP2C-family Ser/Thr protein phosphatase. Structure 12 1947-1954 (2004).
27. Schlicker C. et al. Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: A flexible flap subdomain controls access to the catalytic site. J. Mol. Biol. 376 570-581 (2008).
28. Rayter S. et al. A chemical inhibitor of PPM1D that selectively kills cells overexpressing PPM1D. Oncogene 27 1036-1044 (2008).
29. Kim W. et al. Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol. Cell 44 325-340 (2011).
30. Wagner S.A. et al. A proteome-wide quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol. Cell Proteomics 10 M111.013284 (2011).
31. Ong S.E. The expanding field of SILAC. Anal. Bioanal. Chem. 404 967-976 (2012).
32. Hayashi R. et al. Optimization of a cyclic peptide inhibitor of Ser/Thr phosphatase PPM1D (Wip1). Biochemistry 50 4537-4549 (2011).
33. Tanoue K. et al. Binding of a third metal ion by the human phosphatases PP2Ca and Wip1 is required for phosphatase activity. Biochemistry 52 5830-5843 (2013).