Dipentamethylene thiuram monosulfide is a novel inhibitor of Pin1

Biochemical and Biophysical Research Communications

Volumn 384, Issue 3, 2009, Pages 394-398

  Tatara, Yota ^a   Lin, Yi Chin ^a   Bamba, Yoshimasa ^a   Mori, Tadashi ^a   Uchida, Takafumi ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

Anticancer drug; Dipentamethylene thiuram monosulfide; Docking simulation; FACS; Inhibitor; Pin1; Prolyl isomerase; SPR

Indexed keywords

DIMETHYL SULFOXIDE; DIPENTAMETHYLENE THIURAM MONOSULFIDE; ISOMERASE INHIBITOR; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1; SULFIDE; UNCLASSIFIED DRUG;

ARTICLE; CELL CYCLE ARREST; CELL CYCLE G0 PHASE; CELL STRAIN HCT116; CONTROLLED STUDY; DRUG SCREENING; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME KINETICS; FLUORESCENCE ACTIVATED CELL SORTING; HELA CELL; HUMAN; HUMAN CELL; MOLECULAR MODEL; PRIORITY JOURNAL; SURFACE PLASMON RESONANCE;

ANIMALS; ANTIFUNGAL AGENTS; ANTINEOPLASTIC AGENTS; CATALYTIC DOMAIN; CELL CYCLE; CELL LINE; DRUG DESIGN; ENZYME INHIBITORS; HUMANS; MICE; PEPTIDYLPROLYL ISOMERASE; PIPERIDINES; PROTEIN CONFORMATION; THIRAM;

EUKARYOTA;

EID: 65649122716     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.04.144     Document Type: Article

References (39)

1. Fischer G., Bang H., and Mech C. Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides. Biomed. Biochim. Acta 43 (1984) 1101-1111
2. Lang K., Schmid F.X., and Fischer G. Catalysis of protein folding by prolyl isomerase. Nature 329 (1987) 268-270
3. Bosco D.A., and Kern D. Catalysis and binding of cyclophilin A with different HIV-1 capsid constructs. Biochemistry 43 (2004) 6110-6119
4. 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., Cantley L.C., and Lu K.P. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 278 (1997) 1957-1960
5. Ranganathan R., Lu K.P., Hunter T., and Noel J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89 (1997) 875-886
6. Verdecia M.A., Bowman M.E., Lu K.P., Hunter T., and Noel J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7 (2000) 639-643
7. Crenshaw D.G., Yang J., Means A.R., and Kornbluth S. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17 (1998) 1315-1327
8. Shen M., Stukenberg P.T., Kirschner M.W., and Lu K.P. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12 (1998) 706-720
9. Wells N.J., Watanabe N., Tokusumi T., Jiang W., Verdecia M.A., and 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
10. Messenger M.M., Saulnier R.B., Gilchrist A.D., Diamond P., Gorbsky G.J., and Litchfield D.W. Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions. J. Biol. Chem. 277 (2002) 23054-23064
11. Eckerdt F., Yuan J., Saxena K., Martin B., Kappel S., Lindenau C., Kramer A., Naumann S., Daum S., Fischer G., Dikic I., Kaufmann M., and Strebhardt K. Polo-like kinase 1-mediated phosphorylation stabilizes Pin1 by inhibiting its ubiquitination in human cells. J. Biol. Chem. 280 (2005) 36575-36583
12. Hong J.W., Ryu M.S., and Lim I.K. Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces Pin-1 binding in cytoplasm and cell death. J. Biol. Chem. 280 (2005) 21256-21263
13. Liou Y.C., Ryo A., Huang H.K., Lu P.J., Bronson R., Fujimori F., Uchida T., Hunter T., and 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
14. Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z., Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., and Morrison D.K. Regulation of Raf-1 by direct feedback phosphorylation. Mol. Cell 17 (2005) 215-224
15. Liu W., Youn H.D., Zhou X.Z., Lu K.P., and 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
16. Wulf G.M., Ryo A., Wulf G.G., Lee S.W., Niu T., Petkova V., and 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
17. Monje P., Hernandez Losa J., Lyons R.J., Castellone M.D., and Gutkind J.S. Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1. J. Biol. Chem. 280 (2005) 35081-35084
18. Proteau A., Blier S., Albert A.L., Lavoie S.B., Traish A.M., and Vincent M. The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1. J. Mol. Biol. 346 (2005) 1163-1172
19. Lavoie S.B., Albert A.L., Handa H., Vincent M., and Bensaude O. The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9. J. Mol. Biol. 312 (2001) 675-685
20. Yi P., Wu R.C., Sandquist J., Wong J., Tsai S.Y., Tsai M.J., Means A.R., and O'Malley B.W. Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1). Mol. Cell. Biol. 25 (2005) 9687-9699
21. Albert A.L., Lavoie S., and 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
22. Mantovani F., Piazza S., Gostissa M., Strano S., Zacchi P., Mantovani R., Blandino G., and Del Sal G. Pin1 links the activities of c-Abl and p300 in regulating p73 function. Mol. Cell 14 (2004) 625-636
23. Campaner S., Kaldis P., Izraeli S., and Kirsch I.R. Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint. Mol. Cell. Biol. 25 (2005) 6660-6672
24. Hanes S.D., Shank P.R., and Bostian K.A. Sequence and mutational analysis of ESS1. A gene essential for growth in Saccharomyces cerevisiae. Yeast 5 (1989) 55-72
25. Devasahayam G., Chaturvedi V., and Hanes S.D. The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans. Genetics 160 (2002) 37-48
26. Maleszka R., Hanes S.D., Hackett R.L., de Couet H.G., and 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
27. Fujimori F., Takahashi K., Uchida C., and 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
28. Fujimori F., Gunji W., Kikuchi J., Mogi T., Ohashi Y., Makino T., Oyama A., Okuhara K., Uchida T., and Murakami Y. Crosstalk of prolyl isomerases, Pin1/Ess1, and cyclophilin A. Biochem. Biophys. Res. Commun. 289 (2001) 181-190
29. Liou Y.C., Sun A., Ryo A., Zhou X.Z., Yu Z.X., Huang H.K., Uchida T., Bronson R., Bing G., Li X., Hunter T., and Lu K.P. Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration. Nature 424 (2003) 556-561
30. Akiyama H., Shin R.W., Uchida C., Kitamoto T., and Uchida T. Pin1 promotes production of Alzheimer's amyloid beta from beta-cleaved amyloid precursor protein. Biochem. Biophys. Res. Commun. 336 (2005) 521-529
31. Takahashi K., Akiyama H., Shimazaki K., Uchida C., Akiyama Okunuki H., Tomita M., Fukumoto M., and Uchida T. Ablation of a peptidyl-prolyl isomerase Pin1 from p53-null mice accelerated thymic hyperplasia by increasing the level of the intracellular form of Notch1. Oncogene 26 (2007) 3835-3845
32. Uchida T., Takamiya M., Takahashi M., Miyashita H., Ikeda H., Terada T., Matsuo Y., Shirouzu M., Yokoyama S., Fujimori F., and Hunter T. Pin1 and Par14 peptidyl-prolyl isomerase inhibitors block cell proliferation. Chem. Biol. 10 (2003) 15-24
33. Fanghanel J., Akiyama H., Uchida C., and Uchida T. Comparative analysis of enzyme activities and mRNA levels of peptidyl-prolyl cis/trans isomerases in various organs of wild type and Pin1-/- mice. FEBS Lett. 580 (2006) 3237-3245
34. Nordin H., Jungnelius M., Karlsson R., and Karlsson O.P. Kinetic studies of small molecule interactions with protein kinases using biosensor technology. Anal. Biochem. 340 (2005) 359-368
35. Weiner S.J., Kollman P.A., Case D.A., Singh U.C., and Ghio C. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106 (1984) 765-784
36. Halgren T.A. MMFF VI. MMFF94s option for energy minimization studies. J. Comput. Chem. 20 (1999) 720-729
37. Halgren T.A. MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interraction energies and geometries. J. Comput. Chem. 20 (1999) 730-748
38. Goto J., Kataoka R., Muta H., and Hirayama N. ASEDock-docking based on alpha spheres and excluded volumes. J. Chem. Inf. Model. 48 (2008) 583-590
39. Takahashi K., Uchida C., Shin R.W., Shimazaki K., and Uchida T. Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease. Cell Mol. Life Sci. 65 (2008) 359-375