Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation

Chemistry and Biology

Volumn 10, Issue 1, 2003, Pages 15-24

  Uchida, Takafumi ^a   Takamiya, Mari ^a   Takahashi, Morito ^a   Miyashita, Hitoshi ^a   Ikeda, Hisafumi ^b   Terada, Toru ^c   Matsuo, Yo ^c   Shirouzu, Mikako ^c   Yokoyama, Shigeyuki ^c   Fujimori, Fumihiro ^b   Hunter, Tony ^d  

^a TOHOKU UNIVERSITY   (Japan)

^b TOKYO UNIVERSITY OF SCIENCE   (Japan)

^c RIKEN YOKOHAMA INSTITUTE   (Japan)

^d SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0037256548     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(02)00310-1     Document Type: Article

References (47)

1. Lu K.P., Hanes S.D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:1996;544-547.
2. Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U. Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase. FEBS Lett. 446:1999;278-282.
3. Hanes S.D., Shank P.R., Bostian K.A. Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast. 5:1989;55-72.
4. Hani J., Stumpf G., Domdey H. PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases. FEBS Lett. 365:1995;198-202.
5. Fujimori F., Gunji W., Kikuchi J., Mogi T., Ohashi Y., Makino T., Oyama A., Okuhara K., Uchida T., Murakami Y. Crosstalk of prolyl isomerases, Pin1/Ess1, and Cyclophilin. Biochem. Biophys. Res. Commun. 289:2001;181-190.
6. Huang H.K., Forsburg S.L., John U.P., O'Connell M.J., Hunter T. Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe. J. Cell Sci. 114:2001;3779-3788.
7. Devasahayam G., Chaturvedi V., Hanes S.D. The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans. Genetics. 160:2002;37-48.
8. Maleszka R., Hanes S.D., Hackett R.L., de Couet H.G., Miklos G.L. The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 93:1996;447-451.
9. Kops O., Eckerskorn C., Hottenrott S., Fischer G., Mi H., Tropschug M. Ssp1, a site-specific parvulin homolog from Neurospora crassa active in protein folding. J. Biol. Chem. 273:1998;31971-31976.
10. Fujimori F., Takahashi K., Uchida C., Uchida T. Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest. Biochem. Biophys. Res. Commun. 265:1999;658-663.
11. Sudol M. The WW module competes with the SH3 domain? Trends Biochem. Sci. 21:1996;161-163.
12. Sudol M., Hunter T. New wrinkles for an old domain. Cell. 103:2000;1001-1004.
13. Lu P.J., Zhou X.Z., Shen M., Lu K.P. Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science. 283:1999;1325-1328.
14. Verdecia M.A., Bowman M.E., Lu K.P., Hunter T., Noel J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7:2000;639-643.
15. Crenshaw D.G., Yang J., Means A.R., Kornbluth S. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17:1998;1315-1327.
16. Shen M., Stukenberg P.T., Kirschner M.W., Lu K.P. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12:1998;706-720.
17. Wells N.J., Watanabe N., Tokusumi T., Jiang W., Verdecia M.A., Hunter T. The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression. J. Cell Sci. 112:1999;3361-3371.
18. Stukenberg P.T., Kirschner M.W. Pin1 acts catalytically to promote a conformational change in cdc25. Mol. Cell. 7:2001;1071-1083.
19. Zhou X.Z., Kops O., Werner A., Lu P.J., Shen M., Stoller G., Kullertz G., Stark M., Fischer G., Lu K.P. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and Tau proteins. Mol. Cell. 6:2000;873-883.
20. Lu P.J., Wulf G., Zhou X.Z., Davies P., Lu K.P. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature. 399:1999;784-788.
21. Hsu T., McRackan D., Vincent T.S., Gert De Couet H. Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nat. Cell Biol. 3:2001;538-543.
22. Liu W., Youn H., Zhou X.Z., Lu K.P., Liu J.O. Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. FEBS Lett. 496:2001;105-108.
23. Ryo A., Nakamura M., Wulf G., Liou Y.C., Lu K.P. Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 3:2001;783-801.
24. Wulf G.M., Ryo A., Wulf G.G., Lee S.W., Niu T., Petkova V., Lu K.P. Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. EMBO J. 20:2001;3459-3472.
25. Liou Y.C., Ryo A., Huang H.-K., Lu P.J., Bronson R., Fujimori F., Uchida T., Hunter T., Lu K.P. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc. Natl. Acad. Sci. USA. 99:2002;1335-1340.
26. Miyashita H., Mori S., Motegi K., Fukumoto M., Uchida T. Pin1 is overexpressed in oral squamous cell carcinoma and its level correlates with cyclinD1 level. Oncol. Rep. in press:2002.
27. Albert A., Lavoie S., Vincent M. A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase pin1. J. Cell Sci. 112:1999;2493-2500.
28. Komuro A., Saeki M., Kato S. Npw38, a novel nuclear protein possessing a WW domain capable of activating basal transcription. Nucleic Acids Res. 27:1999;1957-1965.
29. Morris D.P., Phatnani H.P., Greenleaf A.L. Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation. J. Biol. Chem. 274:1999;31583-31587.
30. Hani J., Schelbert B., Bernhardt A., Domdey H., Fischer G., Wiebauer K., Rahfeld J.U. Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3′-end formation of a pre-mRNA in Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;108-116.
31. Wu X., Wilcox C.B., Devasahayam G., Hackett R.L., Arevalo-Rodriguez M., Cardenas M.E., Heitman J., Hanes S.D. The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 19:2000;3727-3738.
32. Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J. Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 19:2000;3739-3749.
33. Gerez L., Mohrmann K., van Raak M., Jongeneelen M., Zhou X.Z., Lu K.P., van Der Sluijs P. Accumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase Pin1 during mitosis. Mol. Biol. Cell. 11:2000;2201-2211.
34. Rippmann J.F., Hobbie S., Daiber C., Guilliard B., Bauer M., Birk J., Nar H., Garin-Chesa P., Rettig W.J., Schnapp A. Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis. Cell Growth Differ. 11:2000;409-416.
35. Yaffe M.B., Schutkowski M., Shen M., Zhou X.Z., Stukenberg P.T., Rahfeld J.-U., Xu J., Kuang J., Kirschner M.W., Fischer G.et al. Sequence-specific and phosphorylation-dependent proline isomerization. a potential mitotic regulatory mechanism Science. 278:1997;1957-1960.
36. Ranganathan R., Lu K.P., Hunter T., Noel J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell. 89:1997;875-886.
37. Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T., Yokoyama S., Uchida T. Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14. J. Mol. Biol. 305:2001;917-926.
38. Sekerina E., Rahfeld J.U., Muller J., Fanghanel J., Rascher C., Fischer G., Bayer P. NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein. J. Mol. Biol. 301:2000;1003-1017.
39. Ewing T.J., Makino S., Skillman A.G., Kuntz I.D. Dock 4.0. search strategies for automated molecular docking of flexible molecule databases J. Comput. Aided Mol. Des. 15:2001;411-428.
40. Jones G., Willett P., Glen R.C. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol. 245:1995;43-53.
41. Jones G., Willet P., Glen R.C., Leach A.R., Taylor R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267:1997;727-748.
42. Rulten S., Thorpe J., Kay J. Identification of eukaryotic parvulin homologues. a new subfamily of peptidylprolyl cis-trans isomerases Biochem. Biophys. Res. Commun. 259:1999;557-562.
43. El-Deiry W.S., Tokino T., Velculescu V.E., Levy D.B., Parsons R., Trent J.M., Lin D., Mercer E., Kinzler K.W., Vogelstein B. WAF1, a potential mediator of p53 tumor suppression. Cell. 75:1993;817-825.
44. Bates S., Rowan S., Vousden K.H. Characterisation of human cyclin G1 and G2. DNA damage inducible genes Oncogene. 13:1996;1103-1109.
45. Hennig L., Christner C., Kipping M., Schelbert B., Rucknagel K.P., Grabley S., Fischer G. Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. Biochemistry. 37:1998;5953-5960.
46. Chao S.H., Greenleaf A.L., Price D.H. Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription. Nucleic Acids Res. 29:2001;767-773.
47. Weinstein I.B. Cancer. Addiction to oncogenes-the Achilles heel of cancer. Science. 297:2002;63-64.