메뉴 건너뛰기




Volumn 388, Issue 10, 2007, Pages 1103-1111

An essential role for Pin1 in Xenopus laevis embryonic development revealed by specific inhibitors

Author keywords

Embryonic development; Inhibition; Microinjection; Peptidyl prolyl cis trans isomerase (PPIase); Phosphopeptide

Indexed keywords

ISOMERASE INHIBITOR; MESSENGER RNA; PEPTIDE DERIVATIVE; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1; PHOSPHOPROTEIN;

EID: 35348853781     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2007.127     Document Type: Article
Times cited : (5)

References (52)
  • 1
    • 0042026692 scopus 로고    scopus 로고
    • Native state proline isomerization: An intrinsic molecular switch
    • Andreotti, A.H. (2003). Native state proline isomerization: an intrinsic molecular switch. Biochemistry 42, 9515-9524.
    • (2003) Biochemistry , vol.42 , pp. 9515-9524
    • Andreotti, A.H.1
  • 2
    • 0242528876 scopus 로고    scopus 로고
    • Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase
    • Arevalo-Rodriguez, M., Cardenas, M.E., Wu, X., Hanes, S.D., and Heitman, J. (2000). Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 19, 3739-3749.
    • (2000) EMBO J , vol.19 , pp. 3739-3749
    • Arevalo-Rodriguez, M.1    Cardenas, M.E.2    Wu, X.3    Hanes, S.D.4    Heitman, J.5
  • 3
    • 33749105127 scopus 로고    scopus 로고
    • A role for Pin1 in mammalian germ cell development and spermatogenesis
    • Atchison, F.W. and Means, A.R. (2004). A role for Pin1 in mammalian germ cell development and spermatogenesis. Front. Biosci. 9, 3248-3256.
    • (2004) Front. Biosci , vol.9 , pp. 3248-3256
    • Atchison, F.W.1    Means, A.R.2
  • 4
    • 0042476570 scopus 로고    scopus 로고
    • Pin1 regulates the timing of mammalian primordial germ cell proliferation
    • Atchison, F.W., Capel, B., and Means, A.R. (2003). Pin1 regulates the timing of mammalian primordial germ cell proliferation. Development 130, 3579-3585.
    • (2003) Development , vol.130 , pp. 3579-3585
    • Atchison, F.W.1    Capel, B.2    Means, A.R.3
  • 5
    • 13244271985 scopus 로고    scopus 로고
    • Identification of hPin1 inhibitors that induce apoptosis in a mammalian Ras transformed cell line
    • Bayer, E., Thutewohl, M., Christner, C., Tradler, T., Osterkamp, F., Waldmann, H., and Bayer, P. (2005). Identification of hPin1 inhibitors that induce apoptosis in a mammalian Ras transformed cell line. Chem. Commun. 4, 516-518.
    • (2005) Chem. Commun , vol.4 , pp. 516-518
    • Bayer, E.1    Thutewohl, M.2    Christner, C.3    Tradler, T.4    Osterkamp, F.5    Waldmann, H.6    Bayer, P.7
  • 6
    • 0033780551 scopus 로고    scopus 로고
    • Signal transduction pathways triggered by fibroblast growth factor receptor 1 expressed in Xenopus laevis oocytes after fibroblast growth factor 1 addition. Role of Grb2, phosphatidylinositol 3-kinase, Src tyrosine kinase, and phospholipase Cγ
    • Browaeys-Poly, E., Cailliau, K., and Vilain, J. (2000). Signal transduction pathways triggered by fibroblast growth factor receptor 1 expressed in Xenopus laevis oocytes after fibroblast growth factor 1 addition. Role of Grb2, phosphatidylinositol 3-kinase, Src tyrosine kinase, and phospholipase Cγ. Eur. J. Biochem. 267, 6256-6263.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6256-6263
    • Browaeys-Poly, E.1    Cailliau, K.2    Vilain, J.3
  • 7
    • 0035253619 scopus 로고    scopus 로고
    • Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription
    • Chao, S.H., Greenleaf, A.L., and Price, D.H. (2001). Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription. Nucleic Acids Res. 29, 767-773.
    • (2001) Nucleic Acids Res , vol.29 , pp. 767-773
    • Chao, S.H.1    Greenleaf, A.L.2    Price, D.H.3
  • 8
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
    • Crenshaw, D.G., Yang, J., Means, A.R., and Kornbluth, S. (1998). The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17, 1315-1327.
    • (1998) EMBO J , vol.17 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 10
    • 33750701178 scopus 로고    scopus 로고
    • Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase Pin1
    • Daum, S., Fanghänel, J., Wildemann, D., and Schiene-Fischer, C. (2006b). Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase Pin1. Biochemistry 45, 12125-12135.
    • (2006) Biochemistry , vol.45 , pp. 12125-12135
    • Daum, S.1    Fanghänel, J.2    Wildemann, D.3    Schiene-Fischer, C.4
  • 11
    • 0036165610 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans
    • Devasahayam, G., Chaturvedi, V., and Hanes, S.D. (2002). The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans. Genetics 160, 37-48.
    • (2002) Genetics , vol.160 , pp. 37-48
    • Devasahayam, G.1    Chaturvedi, V.2    Hanes, S.D.3
  • 12
    • 22144435913 scopus 로고    scopus 로고
    • Prolyl isomerization as a molecular timer in phage infection
    • Eckert, B., Martin, A., Balbach, J., and Schmid, F.X. (2005). Prolyl isomerization as a molecular timer in phage infection. Nat. Struct. Mol. Biol. 12, 619-623.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 619-623
    • Eckert, B.1    Martin, A.2    Balbach, J.3    Schmid, F.X.4
  • 13
    • 1242292029 scopus 로고    scopus 로고
    • Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
    • Fischer, G. and Aumüller, T. (2003). Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Phamacol. 148, 105-150.
    • (2003) Rev. Physiol. Biochem. Phamacol , vol.148 , pp. 105-150
    • Fischer, G.1    Aumüller, T.2
  • 14
    • 0033619755 scopus 로고    scopus 로고
    • Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest
    • Fujimori, F., Takahashi, K., Uchida, C., and Uchida, T. (1999). Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest. Biochem. Biophys. Res. Commun. 265, 658-663.
    • (1999) Biochem. Biophys. Res. Commun , vol.265 , pp. 658-663
    • Fujimori, F.1    Takahashi, K.2    Uchida, C.3    Uchida, T.4
  • 16
    • 17644413069 scopus 로고    scopus 로고
    • Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae
    • Gemmill, T.R., Wu, X., and Hanes, S.D. (2005). Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280, 15510-15517.
    • (2005) J. Biol. Chem , vol.280 , pp. 15510-15517
    • Gemmill, T.R.1    Wu, X.2    Hanes, S.D.3
  • 17
    • 0026145548 scopus 로고
    • Proline-directed protein phosphorylation and cell cycle regulation
    • Hall, F.L. and Vulliet, P.R. (1991). Proline-directed protein phosphorylation and cell cycle regulation. Curr. Opin. Cell Biol. 3, 176-184.
    • (1991) Curr. Opin. Cell Biol , vol.3 , pp. 176-184
    • Hall, F.L.1    Vulliet, P.R.2
  • 18
    • 0024540118 scopus 로고
    • Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae
    • Hanes, S.D., Shank, P.R., and Bostian, K.A. (1989). Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast 5, 55-72.
    • (1989) Yeast , vol.5 , pp. 55-72
    • Hanes, S.D.1    Shank, P.R.2    Bostian, K.A.3
  • 19
    • 0038636446 scopus 로고    scopus 로고
    • Monoclonal antibody against Dnmt1 arrests the cell division of Xenopus early stage embryos
    • Hashimoto, H., Suetake, I., and Tajima, S. (2003). Monoclonal antibody against Dnmt1 arrests the cell division of Xenopus early stage embryos. Exp. Cell Res. 286, 252-262.
    • (2003) Exp. Cell Res , vol.286 , pp. 252-262
    • Hashimoto, H.1    Suetake, I.2    Tajima, S.3
  • 21
    • 0034965466 scopus 로고    scopus 로고
    • Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis
    • Hsu, T., McRackan, D., Vincent, T.S., and Gert de Couet, H. (2001). Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nat. Cell Biol. 3, 538-543.
    • (2001) Nat. Cell Biol , vol.3 , pp. 538-543
    • Hsu, T.1    McRackan, D.2    Vincent, T.S.3    Gert de Couet, H.4
  • 22
    • 0013312518 scopus 로고
    • The translational mobility of substances within the cytoplasmic matrix
    • Jacobson, K. and Woicieszyn, J. (1984). The translational mobility of substances within the cytoplasmic matrix. Proc. Natl. Acad. Sci. USA 81, 6747-6751.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6747-6751
    • Jacobson, K.1    Woicieszyn, J.2
  • 23
    • 0037181170 scopus 로고    scopus 로고
    • Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1
    • Kops, O., Zhou, X.Z., and Lu, K.P. (2002). Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1. FEBS Lett. 513, 305-311.
    • (2002) FEBS Lett , vol.513 , pp. 305-311
    • Kops, O.1    Zhou, X.Z.2    Lu, K.P.3
  • 25
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidylprolyl isomerase essential for regulation of mitosis
    • Lu, K.P, Hanes, S.D., and Hunter, T. (1996). A human peptidylprolyl isomerase essential for regulation of mitosis. Nature 380, 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 26
    • 0036535975 scopus 로고    scopus 로고
    • Pinning down proline-directed phosphorylation signaling
    • Lu, K.P., Liou, Y.C., and Zhou, X.Z. (2002). Pinning down proline-directed phosphorylation signaling. Trends Cell Biol. 12, 164-172.
    • (2002) Trends Cell Biol , vol.12 , pp. 164-172
    • Lu, K.P.1    Liou, Y.C.2    Zhou, X.Z.3
  • 27
    • 33745002500 scopus 로고    scopus 로고
    • Targeting carcinogenesis: A role for the prolyl isomerase Pin1?
    • Lu, K.P., Suizi, F., Zhou, X.Z., Finn, G., Lam, P., and Wulf, G. (2006). Targeting carcinogenesis: a role for the prolyl isomerase Pin1? Mol. Carcinog. 45, 397-402.
    • (2006) Mol. Carcinog , vol.45 , pp. 397-402
    • Lu, K.P.1    Suizi, F.2    Zhou, X.Z.3    Finn, G.4    Lam, P.5    Wulf, G.6
  • 28
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu, P.J., Zhou, X. Z., Shen, M., and Lu, K.P. (1999). Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283, 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 29
    • 0030778411 scopus 로고    scopus 로고
    • The dodo gene family encodes a novel protein involved in signal transduction and protein folding
    • Maleszka, R., Lupas, A., Hanes, S.D., and Miklos, G.L. (1997). The dodo gene family encodes a novel protein involved in signal transduction and protein folding. Gene 203, 89-93.
    • (1997) Gene , vol.203 , pp. 89-93
    • Maleszka, R.1    Lupas, A.2    Hanes, S.D.3    Miklos, G.L.4
  • 30
    • 0031581055 scopus 로고    scopus 로고
    • Xenopus FK 506-binding protein homolog induces a secondary axis in frog embryos, which is inhibited by coexisting BMP 4 signaling
    • Nishinakamura, R., Matsumoto, Y., Uochi, T., Asashima, M., and Yokota, T. (1997). Xenopus FK 506-binding protein homolog induces a secondary axis in frog embryos, which is inhibited by coexisting BMP 4 signaling. Biochem. Biophys. Res. Commun. 239, 585-591.
    • (1997) Biochem. Biophys. Res. Commun , vol.239 , pp. 585-591
    • Nishinakamura, R.1    Matsumoto, Y.2    Uochi, T.3    Asashima, M.4    Yokota, T.5
  • 32
    • 33645300736 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production
    • Pastorino, L., Sun, A., Lu, P.J., Zhou, X.Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S.H., Li, X., et al. (2006). The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440, 528-534.
    • (2006) Nature , vol.440 , pp. 528-534
    • Pastorino, L.1    Sun, A.2    Lu, P.J.3    Zhou, X.Z.4    Balastik, M.5    Finn, G.6    Wulf, G.7    Lim, J.8    Li, S.H.9    Li, X.10
  • 33
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions
    • Pearson, G., Robinson, F., Gibson, T.B., Xu, B.E., Karandikar, M., Berman, K., and Cobb, M.H. (2001). Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr. Rev. 22, 153-183.
    • (2001) Endocr. Rev , vol.22 , pp. 153-183
    • Pearson, G.1    Robinson, F.2    Gibson, T.B.3    Xu, B.E.4    Karandikar, M.5    Berman, K.6    Cobb, M.H.7
  • 34
    • 33344472738 scopus 로고    scopus 로고
    • Molecular details of Itk activation by prolyl isomerization and phospholigand binding: The NMR structure of the Itk SH2 domain bound to a phosphopeptide
    • Pletneva, E.V., Sundd, M., Fulton, D.B., and Andreotti, A.H. (2006). Molecular details of Itk activation by prolyl isomerization and phospholigand binding: the NMR structure of the Itk SH2 domain bound to a phosphopeptide. J. Mol. Biol. 357, 550-561.
    • (2006) J. Mol. Biol , vol.357 , pp. 550-561
    • Pletneva, E.V.1    Sundd, M.2    Fulton, D.B.3    Andreotti, A.H.4
  • 35
    • 0037007447 scopus 로고    scopus 로고
    • Local structural changes caused by peptidyl-prolyl cis/trans isomerization in the native state of proteins
    • Reimer, U. and Fischer, G. (2002). Local structural changes caused by peptidyl-prolyl cis/trans isomerization in the native state of proteins. Biophys. Chem. 96, 203-212.
    • (2002) Biophys. Chem , vol.96 , pp. 203-212
    • Reimer, U.1    Fischer, G.2
  • 37
    • 0033574995 scopus 로고    scopus 로고
    • Identification of eukaryotic parvulin homologues: A new subfamily of peptidylprolyl cis-trans isomerases
    • Rulten, S., Thorpe, J., and Kay, J. (1999). Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases. Biochim. Biophys. Res. Commun. 259, 557-562.
    • (1999) Biochim. Biophys. Res. Commun , vol.259 , pp. 557-562
    • Rulten, S.1    Thorpe, J.2    Kay, J.3
  • 38
    • 0036315162 scopus 로고    scopus 로고
    • PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells
    • Ryo, A., Liou, Y.C., Wulf, G., Nakamura, M., Lee, S.W., and Lu, K.P. (2002). PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell. Biol. 22, 5281-5295.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5281-5295
    • Ryo, A.1    Liou, Y.C.2    Wulf, G.3    Nakamura, M.4    Lee, S.W.5    Lu, K.P.6
  • 39
    • 0037351048 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1: A catalyst for oncogenesis and a potential therapeutic target in cancer
    • Ryo, A., Liou, Y.C., Lu, K.P., and Wulf, G. (2003). Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer. J. Cell Sci. 116, 773-783.
    • (2003) J. Cell Sci , vol.116 , pp. 773-783
    • Ryo, A.1    Liou, Y.C.2    Lu, K.P.3    Wulf, G.4
  • 40
    • 0034840950 scopus 로고    scopus 로고
    • Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC
    • Ryo, A., Nakamura, M., Wulf, G., Liou, Y.C., and Lu, K.P. (2001). Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 3, 793-801.
    • (2001) Nat. Cell Biol , vol.3 , pp. 793-801
    • Ryo, A.1    Nakamura, M.2    Wulf, G.3    Liou, Y.C.4    Lu, K.P.5
  • 41
    • 0032031634 scopus 로고    scopus 로고
    • The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins
    • Shen, M.H., Stukenberg, P.T., Kirschner, M.W., and Lu, K.P. (1998). The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12, 706-720.
    • (1998) Genes Dev , vol.12 , pp. 706-720
    • Shen, M.H.1    Stukenberg, P.T.2    Kirschner, M.W.3    Lu, K.P.4
  • 42
    • 0034212392 scopus 로고    scopus 로고
    • Xenopus FK506-binding protein, a novel immunophilin expressed during early development
    • Spokony, R. and Saint-Jeannet, J.P. (2000). Xenopus FK506-binding protein, a novel immunophilin expressed during early development. Mech. Dev. 94, 205-208.
    • (2000) Mech. Dev , vol.94 , pp. 205-208
    • Spokony, R.1    Saint-Jeannet, J.P.2
  • 43
    • 33749080161 scopus 로고    scopus 로고
    • Subtilisin-like proprotein convertase activity is necessary for left-right axis determination in Xenopus neurula embryos
    • Toyoizumi, R., Takeuchi, S., and Mogi, K. (2006). Subtilisin-like proprotein convertase activity is necessary for left-right axis determination in Xenopus neurula embryos. Dev. Genes Evol. 216, 607-622.
    • (2006) Dev. Genes Evol , vol.216 , pp. 607-622
    • Toyoizumi, R.1    Takeuchi, S.2    Mogi, K.3
  • 44
    • 0033039865 scopus 로고    scopus 로고
    • Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase
    • Uchida, T., Fujimori, F., Tradler, T., Fischer, G., and Rahfeld, J.U. (1999). Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase. FEBS Lett. 446, 278-282.
    • (1999) FEBS Lett , vol.446 , pp. 278-282
    • Uchida, T.1    Fujimori, F.2    Tradler, T.3    Fischer, G.4    Rahfeld, J.U.5
  • 46
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T., and Noel, J.P. (2000). Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7, 639-643.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 47
    • 9644302270 scopus 로고    scopus 로고
    • Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere
    • Wang, X.J., Xu, B., Mullins, A.B., Neiler, F.K., and Etzkorn, F.A. (2004). Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere. J. Am. Chem. Soc. 126, 15533-15542.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15533-15542
    • Wang, X.J.1    Xu, B.2    Mullins, A.B.3    Neiler, F.K.4    Etzkorn, F.A.5
  • 48
    • 0342322902 scopus 로고    scopus 로고
    • Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase
    • Weiwad, M., Küllertz, G., Schutkowski, M., and Fischer, G. (2000). Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase. FEBS Lett. 478, 39-42.
    • (2000) FEBS Lett , vol.478 , pp. 39-42
    • Weiwad, M.1    Küllertz, G.2    Schutkowski, M.3    Fischer, G.4
  • 50
    • 0034050649 scopus 로고    scopus 로고
    • Requirement of the prolyl isomerase Pin1 for the replication checkpoint
    • Winkler, K.E., Swenson, K.I., Kornbluth, S., and Means, A.R. (2000). Requirement of the prolyl isomerase Pin1 for the replication checkpoint. Science 287, 1644-1647.
    • (2000) Science , vol.287 , pp. 1644-1647
    • Winkler, K.E.1    Swenson, K.I.2    Kornbluth, S.3    Means, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.