메뉴 건너뛰기




Volumn 1842, Issue 2, 2014, Pages 154-163

The Stress-response protein prostate-associated gene 4, interacts with c-Jun and potentiates its transactivation

Author keywords

C Jun; Cancer Testis Antigen; Intrinsically disordered protein; PAGE4; Prostate cancer; SmFRET

Indexed keywords

CARDIOLIPIN; DNA; HEAT SHOCK PROTEIN; PROSTATE ASSOCIATED GENE 4; PROSTATE PROTEIN; PROTEIN C JUN; REACTIVE OXYGEN METABOLITE; RECOMBINANT PROTEIN; STRESS RESPONSE PROTEIN PROSTATE ASSOCIATED GENE 4; UNCLASSIFIED DRUG;

EID: 84890141083     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2013.11.014     Document Type: Article
Times cited : (35)

References (70)
  • 3
    • 0036813331 scopus 로고    scopus 로고
    • Cancer/testis antigens: an expanding family of targets for cancer immunotherapy
    • Scanlan M.J., Gure A.O., Jungbluth A.A., Old L.J., Chen Y.T. Cancer/testis antigens: an expanding family of targets for cancer immunotherapy. Immunol. Rev. 2002, 188:22-32.
    • (2002) Immunol. Rev. , vol.188 , pp. 22-32
    • Scanlan, M.J.1    Gure, A.O.2    Jungbluth, A.A.3    Old, L.J.4    Chen, Y.T.5
  • 5
    • 84866499457 scopus 로고    scopus 로고
    • PAGE4 positivity is associated with attenuated AR signaling and predicts patient survival in hormone-naive prostate cancer
    • Sampson N., Ruiz C., Zenzmaier C., Bubendorf L., Berger P. PAGE4 positivity is associated with attenuated AR signaling and predicts patient survival in hormone-naive prostate cancer. Am. J. Pathol. 2012, 181:1443-1454.
    • (2012) Am. J. Pathol. , vol.181 , pp. 1443-1454
    • Sampson, N.1    Ruiz, C.2    Zenzmaier, C.3    Bubendorf, L.4    Berger, P.5
  • 8
    • 79954627742 scopus 로고    scopus 로고
    • The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein
    • Zeng Y., He Y., Yang F., Mooney S.M., Getzenberg R.H., Orban J., Kulkarni P. The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. J. Biol. Chem. 2011, 286:13985-13994.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13985-13994
    • Zeng, Y.1    He, Y.2    Yang, F.3    Mooney, S.M.4    Getzenberg, R.H.5    Orban, J.6    Kulkarni, P.7
  • 9
    • 84876281768 scopus 로고    scopus 로고
    • Unusual biophysics of intrinsically disordered proteins
    • Uversky V.N. Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta 2013, 1834:932-951.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 932-951
    • Uversky, V.N.1
  • 10
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: a 10-year recap
    • Tompa P. Intrinsically disordered proteins: a 10-year recap. Trends Biochem. Sci. 2012, 37:509-516.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 509-516
    • Tompa, P.1
  • 11
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: introducing the D2 concept
    • Uversky V.N., Oldfield C.J., Dunker A.K. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu. Rev. Biophys. 2008, 37:215-246.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 12
    • 77951898121 scopus 로고    scopus 로고
    • Hub promiscuity in protein-protein interaction networks
    • Patil A., Kinoshita K., Nakamura H. Hub promiscuity in protein-protein interaction networks. Int. J. Mol. Sci. 2010, 11:1930-1943.
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 1930-1943
    • Patil, A.1    Kinoshita, K.2    Nakamura, H.3
  • 14
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P., Csermely P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J. 2004, 18:1169-1175.
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 15
    • 66749163093 scopus 로고    scopus 로고
    • Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data
    • Edwards Y.J., Lobley A.E., Pentony M.M., Jones D.T. Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data. Genome Biol. 2009, 10:R50.
    • (2009) Genome Biol. , vol.10
    • Edwards, Y.J.1    Lobley, A.E.2    Pentony, M.M.3    Jones, D.T.4
  • 17
    • 60149111586 scopus 로고    scopus 로고
    • Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition
    • Yoon M.K., Venkatachalam V., Huang A., Choi B.S., Stultz C.M., Chou J.J. Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition. Protein Sci. 2009, 18:337-347.
    • (2009) Protein Sci. , vol.18 , pp. 337-347
    • Yoon, M.K.1    Venkatachalam, V.2    Huang, A.3    Choi, B.S.4    Stultz, C.M.5    Chou, J.J.6
  • 19
    • 45849117986 scopus 로고    scopus 로고
    • Backbone dynamics of the 18.5kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site
    • Libich D.S., Harauz G. Backbone dynamics of the 18.5kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site. Biophys. J. 2008, 94:4847-4866.
    • (2008) Biophys. J. , vol.94 , pp. 4847-4866
    • Libich, D.S.1    Harauz, G.2
  • 20
    • 78650590282 scopus 로고    scopus 로고
    • Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation
    • Lee C.W., Ferreon J.C., Ferreon A.C., Arai M., Wright P.E. Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:19290-19295.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 19290-19295
    • Lee, C.W.1    Ferreon, J.C.2    Ferreon, A.C.3    Arai, M.4    Wright, P.E.5
  • 21
    • 64349086059 scopus 로고    scopus 로고
    • Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP
    • Lee C.W., Arai M., Martinez-Yamout M.A., Dyson H.J., Wright P.E. Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP. Biochemistry 2009, 48:2115-2124.
    • (2009) Biochemistry , vol.48 , pp. 2115-2124
    • Lee, C.W.1    Arai, M.2    Martinez-Yamout, M.A.3    Dyson, H.J.4    Wright, P.E.5
  • 23
    • 78751591016 scopus 로고    scopus 로고
    • Segmental conformational disorder and dynamics in the intrinsically disordered protein alpha-synuclein and its chain length dependence
    • Grupi A., Haas E. Segmental conformational disorder and dynamics in the intrinsically disordered protein alpha-synuclein and its chain length dependence. J. Mol. Biol. 2011, 405:1267-1283.
    • (2011) J. Mol. Biol. , vol.405 , pp. 1267-1283
    • Grupi, A.1    Haas, E.2
  • 24
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence
    • Ferreon A.C., Gambin Y., Lemke E.A., Deniz A.A. Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:5645-5650.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5645-5650
    • Ferreon, A.C.1    Gambin, Y.2    Lemke, E.A.3    Deniz, A.A.4
  • 26
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri T., Semple J.I., Garcia-Verdugo R., Lehner B. Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 2009, 138:198-208.
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 28
    • 67649654466 scopus 로고    scopus 로고
    • Disorder, promiscuity, and toxic partnerships
    • Marcotte E.M., Tsechansky M. Disorder, promiscuity, and toxic partnerships. Cell 2009, 138:16-18.
    • (2009) Cell , vol.138 , pp. 16-18
    • Marcotte, E.M.1    Tsechansky, M.2
  • 29
    • 84859641038 scopus 로고    scopus 로고
    • Using gene expression noise to understand gene regulation
    • Munsky B., Neuert G., van Oudenaarden A. Using gene expression noise to understand gene regulation. Science 2012, 336:183-187.
    • (2012) Science , vol.336 , pp. 183-187
    • Munsky, B.1    Neuert, G.2    van Oudenaarden, A.3
  • 30
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi Y., Choi P.J., Li G.W., Chen H., Babu M., Hearn J., Emili A., Xie X.S. Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 2010, 329:533-538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4    Babu, M.5    Hearn, J.6    Emili, A.7    Xie, X.S.8
  • 31
    • 84860527594 scopus 로고    scopus 로고
    • Noise in cellular signaling pathways: causes and effects
    • Ladbury J.E., Arold S.T. Noise in cellular signaling pathways: causes and effects. Trends Biochem. Sci. 2012, 37:173-178.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 173-178
    • Ladbury, J.E.1    Arold, S.T.2
  • 33
    • 77957287427 scopus 로고    scopus 로고
    • Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA helicase
    • Mooney S.M., Goel A., D'Assoro A.B., Salisbury J.L., Janknecht R. Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA helicase. J. Biol. Chem. 2010, 285:30443-30452.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30443-30452
    • Mooney, S.M.1    Goel, A.2    D'Assoro, A.B.3    Salisbury, J.L.4    Janknecht, R.5
  • 35
    • 0037064027 scopus 로고    scopus 로고
    • The ferroxidase activity of yeast frataxin
    • Park S., Gakh O., Mooney S.M., Isaya G. The ferroxidase activity of yeast frataxin. J. Biol. Chem. 2002, 277:38589-38595.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38589-38595
    • Park, S.1    Gakh, O.2    Mooney, S.M.3    Isaya, G.4
  • 38
    • 79953838275 scopus 로고    scopus 로고
    • Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins
    • Choi U.B., McCann J.J., Weninger K.R., Bowen M.E. Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. Structure 2011, 19:566-576.
    • (2011) Structure , vol.19 , pp. 566-576
    • Choi, U.B.1    McCann, J.J.2    Weninger, K.R.3    Bowen, M.E.4
  • 39
    • 84865345067 scopus 로고    scopus 로고
    • Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics
    • Choi U.B., Weninger K.R., Bowen M.E. Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics. Methods Mol. Biol. 2012, 896:3-20.
    • (2012) Methods Mol. Biol. , vol.896 , pp. 3-20
    • Choi, U.B.1    Weninger, K.R.2    Bowen, M.E.3
  • 40
    • 34548792937 scopus 로고    scopus 로고
    • Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events
    • Li Y., Augustine G.J., Weninger K. Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events. Biophys. J. 2007, 93:2178-2187.
    • (2007) Biophys. J. , vol.93 , pp. 2178-2187
    • Li, Y.1    Augustine, G.J.2    Weninger, K.3
  • 41
    • 77955700423 scopus 로고    scopus 로고
    • Optimizing methods to recover absolute FRET efficiency from immobilized single molecules
    • McCann J.J., Choi U.B., Zheng L., Weninger K., Bowen M.E. Optimizing methods to recover absolute FRET efficiency from immobilized single molecules. Biophys. J. 2010, 99:961-970.
    • (2010) Biophys. J. , vol.99 , pp. 961-970
    • McCann, J.J.1    Choi, U.B.2    Zheng, L.3    Weninger, K.4    Bowen, M.E.5
  • 42
    • 25844444803 scopus 로고    scopus 로고
    • Photon counting histograms for diffusing fluorophores
    • Gopich I.V., Szabo A. Photon counting histograms for diffusing fluorophores. J. Phys. Chem. B 2005, 109:17683-17688.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 17683-17688
    • Gopich, I.V.1    Szabo, A.2
  • 43
    • 73449119972 scopus 로고    scopus 로고
    • Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential
    • Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R. Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential. Biochemistry 2010, 49:1-10.
    • (2010) Biochemistry , vol.49 , pp. 1-10
    • Mooney, S.M.1    Grande, J.P.2    Salisbury, J.L.3    Janknecht, R.4
  • 44
    • 34548168073 scopus 로고    scopus 로고
    • MiR-221 and miR-222 expression affects the proliferation potential of human prostate carcinoma cell lines by targeting p27Kip1
    • Galardi S., Mercatelli N., Giorda E., Massalini S., Frajese G.V., Ciafre S.A., Farace M.G. miR-221 and miR-222 expression affects the proliferation potential of human prostate carcinoma cell lines by targeting p27Kip1. J. Biol. Chem. 2007, 23716-23724.
    • (2007) J. Biol. Chem. , pp. 23716-23724
    • Galardi, S.1    Mercatelli, N.2    Giorda, E.3    Massalini, S.4    Frajese, G.V.5    Ciafre, S.A.6    Farace, M.G.7
  • 47
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 2002, 11:739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 48
    • 30344473311 scopus 로고    scopus 로고
    • Organized arrays of individual DNA molecules tethered to supported lipid bilayers
    • Graneli A., Yeykal C.C., Prasad T.K., Greene E.C. Organized arrays of individual DNA molecules tethered to supported lipid bilayers. Langmuir 2006, 22:292-299.
    • (2006) Langmuir , vol.22 , pp. 292-299
    • Graneli, A.1    Yeykal, C.C.2    Prasad, T.K.3    Greene, E.C.4
  • 49
    • 0035819204 scopus 로고    scopus 로고
    • Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy
    • Boukobza E., Sonnenfeld A., Haran G. Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy. J. Phys. Chem. B 2001, 105:12165-12170.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12165-12170
    • Boukobza, E.1    Sonnenfeld, A.2    Haran, G.3
  • 53
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins D.K., Grimshaw S.B., Receveur V., Dobson C.M., Jones J.A., Smith L.J. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 1999, 38:16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 57
  • 61
    • 79954987841 scopus 로고    scopus 로고
    • NF-kB and c-Jun induce the expression of the oncogenic miR-221 and miR-222 in prostate carcinoma and glioblastoma cells
    • Galardi S., Mercatelli N., Farace M.G., Ciafre S.A. NF-kB and c-Jun induce the expression of the oncogenic miR-221 and miR-222 in prostate carcinoma and glioblastoma cells. Nucleic Acids Res. 2011, 39:3892-3902.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 3892-3902
    • Galardi, S.1    Mercatelli, N.2    Farace, M.G.3    Ciafre, S.A.4
  • 62
    • 0030841919 scopus 로고    scopus 로고
    • Androgenic induction of prostate-specific antigen gene is repressed by protein-protein interaction between the androgen receptor and AP-1/c-Jun in the human prostate cancer cell line LNCaP
    • Sato N., Sadar M.D., Bruchovsky N., Saatcioglu F., Rennie P.S., Sato S., Lange P.H., Gleave M.E. Androgenic induction of prostate-specific antigen gene is repressed by protein-protein interaction between the androgen receptor and AP-1/c-Jun in the human prostate cancer cell line LNCaP. J. Biol. Chem. 1997, 272:17485-17494.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17485-17494
    • Sato, N.1    Sadar, M.D.2    Bruchovsky, N.3    Saatcioglu, F.4    Rennie, P.S.5    Sato, S.6    Lange, P.H.7    Gleave, M.E.8
  • 63
    • 33751102108 scopus 로고    scopus 로고
    • C-Jun enhancement of androgen receptor transactivation is associated with prostate cancer cell proliferation
    • Chen S.Y., Cai C., Fisher C.J., Zheng Z., Omwancha J., Hsieh C.L., Shemshedini L. c-Jun enhancement of androgen receptor transactivation is associated with prostate cancer cell proliferation. Oncogene 2006, 25:7212-7223.
    • (2006) Oncogene , vol.25 , pp. 7212-7223
    • Chen, S.Y.1    Cai, C.2    Fisher, C.J.3    Zheng, Z.4    Omwancha, J.5    Hsieh, C.L.6    Shemshedini, L.7
  • 64
    • 34547116209 scopus 로고    scopus 로고
    • C-Jun has multiple enhancing activities in the novel cross talk between the androgen receptor and Ets variant gene 1 in prostate cancer
    • Cai C., Hsieh C.L., Shemshedini L. c-Jun has multiple enhancing activities in the novel cross talk between the androgen receptor and Ets variant gene 1 in prostate cancer. Mol. Cancer Res. 2007, 5:725-735.
    • (2007) Mol. Cancer Res. , vol.5 , pp. 725-735
    • Cai, C.1    Hsieh, C.L.2    Shemshedini, L.3
  • 65
    • 35348861265 scopus 로고    scopus 로고
    • Stromally expressed c-Jun regulates proliferation of prostate epithelial cells
    • Li W., Wu C.L., Febbo P.G., Olumi A.F. Stromally expressed c-Jun regulates proliferation of prostate epithelial cells. Am. J. Pathol. 2007, 171:1189-1198.
    • (2007) Am. J. Pathol. , vol.171 , pp. 1189-1198
    • Li, W.1    Wu, C.L.2    Febbo, P.G.3    Olumi, A.F.4
  • 66
    • 5044238301 scopus 로고    scopus 로고
    • The role of c-Jun and c-Fos expression in androgen-independent prostate cancer
    • Edwards J., Krishna N.S., Mukherjee R., Bartlett J.M. The role of c-Jun and c-Fos expression in androgen-independent prostate cancer. J. Pathol. 2004, 204:153-158.
    • (2004) J. Pathol. , vol.204 , pp. 153-158
    • Edwards, J.1    Krishna, N.S.2    Mukherjee, R.3    Bartlett, J.M.4
  • 67
    • 84861576642 scopus 로고    scopus 로고
    • The altered expression of MiR-221/-222 and MiR-23b/-27b is associated with the development of human castration resistant prostate cancer
    • Sun T., Yang M., Chen S., Balk S., Pomerantz M., Hsieh C.L., Brown M., Lee G.S., Kantoff P.W. The altered expression of MiR-221/-222 and MiR-23b/-27b is associated with the development of human castration resistant prostate cancer. Prostate 2012, 72:1093-1103.
    • (2012) Prostate , vol.72 , pp. 1093-1103
    • Sun, T.1    Yang, M.2    Chen, S.3    Balk, S.4    Pomerantz, M.5    Hsieh, C.L.6    Brown, M.7    Lee, G.S.8    Kantoff, P.W.9
  • 70
    • 0036275438 scopus 로고    scopus 로고
    • An essential function of AP-1 heterodimers in Drosophila development
    • Ciapponi L., Bohmann D. An essential function of AP-1 heterodimers in Drosophila development. Mech. Dev. 2002, 115:35-40.
    • (2002) Mech. Dev. , vol.115 , pp. 35-40
    • Ciapponi, L.1    Bohmann, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.