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Volumn 12, Issue 2, 2007, Pages 700-711

Ubiquitin-like protein modifications in prostate and breast cancer

Author keywords

Posttranslational modification; Prostate cancer and breast cancer; Sumoylation; Ubc9; Ubiquitin like protein

Indexed keywords


EID: 34249796386     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/2094     Document Type: Article
Times cited : (20)

References (119)
  • 1
    • 0038066613 scopus 로고    scopus 로고
    • The role of the ubiquitination-proteasome pathway in breast cancer: Ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer
    • Lipkowitz, S.: The role of the ubiquitination-proteasome pathway in breast cancer: ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer. Breast Cancer Res, 5, 8-15 (2003)
    • (2003) Breast Cancer Res , vol.5 , pp. 8-15
    • Lipkowitz, S.1
  • 2
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • Gill, G.: SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev, 18, 2046-59 (2004)
    • (2004) Genes Dev , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 3
    • 0034523266 scopus 로고    scopus 로고
    • SUMO-nonclassical ubiquitin
    • Melchior, F.: SUMO-nonclassical ubiquitin. Annu Rev Cell Dev Biol, 16, 591-626 (2000)
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 591-626
    • Melchior, F.1
  • 4
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S.: Protein modification by SUMO. Annu Rev Biochem, 73, 355-82 (2004)
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 6
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of SUMO
    • Seeler, J. S. & A. Dejean: Nuclear and unclear functions of SUMO. Nat Rev Mol Cell Biol, 4, 690-9 (2003)
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 690-699
    • Seeler, J.S.1    Dejean, A.2
  • 7
    • 9644278013 scopus 로고    scopus 로고
    • SUMO protein modification
    • Dohmen, R. J.: SUMO protein modification. Biochim Biophys Acta, 1695, 113-31 (2004)
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 113-131
    • Dohmen, R.J.1
  • 9
    • 0035852990 scopus 로고    scopus 로고
    • Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein
    • Jin, C., T. Shiyanova, Z. Shen & X. Liao: Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein. Int J Biol Macromol, 28, 227-34 (2001)
    • (2001) Int J Biol Macromol , vol.28 , pp. 227-234
    • Jin, C.1    Shiyanova, T.2    Shen, Z.3    Liao, X.4
  • 11
  • 14
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh, H. & J. Hinchey: Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem, 275, 6252-8 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 15
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • Bylebyl, G. R., I. Belichenko & E. S. Johnson: The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J Biol Chem, 278, 44113-20 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 16
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E. S., I. Schwienhorst, R. J. Dohmen & G. Blobel: The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. Embo J, 16, 5509-19 (1997)
    • (1997) Embo J , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 19
    • 0037033071 scopus 로고    scopus 로고
    • Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation
    • Bencsath, K. P., M. S. Podgorski, V. R. Pagala, C. A. Slaughter & B. A. Schulman: Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation. J Biol Chem, 277, 47938-45 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 47938-47945
    • Bencsath, K.P.1    Podgorski, M.S.2    Pagala, V.R.3    Slaughter, C.A.4    Schulman, B.A.5
  • 20
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M. S., C. Dargemont & R. T. Hay: SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem, 276, 12654-9 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 21
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor, V., D. A. Sampson, M. J. Matunis & C. D. Lima: Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell, 108, 345-56 (2002)
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 22
    • 0037077265 scopus 로고    scopus 로고
    • Identification of a substrate recognition site on Ubc9
    • Lin, D., M. H. Tatham, B. Yu, S. Kim, R. T. Hay & Y. Chen: Identification of a substrate recognition site on Ubc9. J Biol Chem, 277, 21740-8 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 21740-21748
    • Lin, D.1    Tatham, M.H.2    Yu, B.3    Kim, S.4    Hay, R.T.5    Chen, Y.6
  • 23
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • Giorgino, F., O. de Robertis, L. Laviola, C. Montrone, S. Perrini, K. C. McCowen & R. J. Smith: The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc Natl Acad Sci U S A, 97, 1125-30 (2000)
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1125-1130
    • Giorgino, F.1    de Robertis, O.2    Laviola, L.3    Montrone, C.4    Perrini, S.5    McCowen, K.C.6    Smith, R.J.7
  • 24
    • 0037169534 scopus 로고    scopus 로고
    • Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein
    • Mo, Y. Y., Y. Yu, Z. Shen & W. T. Beck: Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein. J Biol Chem, 211, 2958-64 (2002)
    • (2002) J Biol Chem , vol.211 , pp. 2958-2964
    • Mo, Y.Y.1    Yu, Y.2    Shen, Z.3    Beck, W.T.4
  • 25
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson, E. S. & A. A. Gupta: An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell, 106, 735-44 (2001)
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 26
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo, T., T. Nishida & H. Yasuda: Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol Cell, 8, 713-8 (2001)
    • (2001) Mol Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 27
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler, A., A. Gast, J. S. Seeler, A. Dejean & F. Melchior: The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell, 108, 109-20 (2002)
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 28
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey, M. H., T. A. Melhuish & D. Wotton: The polycomb protein Pc2 is a SUMO E3. Cell, 113, 127-37 (2003)
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 29
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S. J. & M. Hochstrasser: A new protease required for cell-cycle progression in yeast. Nature, 398, 246-51 (1999)
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 30
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • Li, S. J. & M. Hochstrasser: The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol Cell Biol, 20, 2367-77 (2000)
    • (2000) Mol Cell Biol , vol.20 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 31
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin-specific protease
    • Gong, L., S. Millas, G. G. Maul & E. T. Yeh: Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem, 215, 3355-9 (2000)
    • (2000) J Biol Chem , vol.215 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 32
    • 0035914357 scopus 로고    scopus 로고
    • Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation
    • Nishida, T., F. Kaneko, M. Kitagawa & H. Yasuda: Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation. J Biol Chem, 276, 39060-6 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 39060-39066
    • Nishida, T.1    Kaneko, F.2    Kitagawa, M.3    Yasuda, H.4
  • 33
    • 0033760171 scopus 로고    scopus 로고
    • A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase
    • Nishida, T., H. Tanaka & H. Yasuda: A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. Eur J Biochem, 267, 6423-7 (2000)
    • (2000) Eur J Biochem , vol.267 , pp. 6423-6427
    • Nishida, T.1    Tanaka, H.2    Yasuda, H.3
  • 34
    • 0036939820 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICPO co-localizes with a SUMO-specific protease
    • Bailey, D. & P. O'Hare: Herpes simplex virus 1 ICPO co-localizes with a SUMO-specific protease. J Gen Virol, 83, 2951-64 (2002)
    • (2002) J Gen Virol , vol.83 , pp. 2951-2964
    • Bailey, D.1    O'Hare, P.2
  • 35
    • 0037205460 scopus 로고    scopus 로고
    • Association of the human SUMO-1 protease SENP2 with the nuclear pore
    • Hang, J. & M. Dasso: Association of the human SUMO-1 protease SENP2 with the nuclear pore. J Biol Chem, 211, 19961-6 (2002)
    • (2002) J Biol Chem , vol.211 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 36
    • 14644392172 scopus 로고    scopus 로고
    • Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome
    • Wykoff, D. D. & E. K. O'Shea: Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome. Mol Cell Proteomics, 4, 73-83 (2005)
    • (2005) Mol Cell Proteomics , vol.4 , pp. 73-83
    • Wykoff, D.D.1    O'Shea, E.K.2
  • 37
    • 20444375092 scopus 로고    scopus 로고
    • A genome-wide analysis of sumoylation-related biological processes and functions in human nucleus
    • Zhou, F., Y. Xue, H. Lu, G. Chen & X. Yao: A genome-wide analysis of sumoylation-related biological processes and functions in human nucleus. FEBS Lett, 579, 3369-75 (2005)
    • (2005) FEBS Lett , vol.579 , pp. 3369-3375
    • Zhou, F.1    Xue, Y.2    Lu, H.3    Chen, G.4    Yao, X.5
  • 38
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., E. Coutavas & G. Blobel: A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol, 135, 1457-70 (1996)
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 39
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., C. Delphin, T. Guan, L. Gerace & F. Melchior: A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell, 88, 97-107 (1997)
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 41
    • 0035949590 scopus 로고    scopus 로고
    • SUMO-1 modification required for transformation by adenovirus type 5 early region IB 55-kDa oncoprotein
    • Endter, C., J. Kzhyshkowska, R. Stauber & T. Dobner: SUMO-1 modification required for transformation by adenovirus type 5 early region IB 55-kDa oncoprotein. Proc Natl Acad Sei USA, 98, 11312-7 (2001)
    • (2001) Proc Natl Acad Sei USA , vol.98 , pp. 11312-11317
    • Endter, C.1    Kzhyshkowska, J.2    Stauber, R.3    Dobner, T.4
  • 42
    • 0037417957 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier-1 modification mediates resolution of CREB-dependent responses to hypoxia
    • Comerford, K. M., M. O. Leonard, J. Karhausen, R. Carey, S. P. Colgan & C. T. Taylor: Small ubiquitin-related modifier-1 modification mediates resolution of CREB-dependent responses to hypoxia. Proc Natl Acad Sci USA, 100, 986-91 (2003)
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 986-991
    • Comerford, K.M.1    Leonard, M.O.2    Karhausen, J.3    Carey, R.4    Colgan, S.P.5    Taylor, C.T.6
  • 43
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress
    • Huang, T. T., S. M. Wuerzberger-Davis, Z. H. Wu & S. Miyamoto: Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell, 115, 565-76 (2003)
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 46
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: A model for nuclear organelles
    • Lamond, A. I. & D. L. Specter: Nuclear speckles: a model for nuclear organelles. Nat Rev Mol Cell Biol, 4, 605-12 (2003)
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 605-612
    • Lamond, A.I.1    Specter, D.L.2
  • 49
    • 0037131273 scopus 로고    scopus 로고
    • Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin
    • Rallabhandi, P., K. Hashimoto, Y. Y. Mo, W. T. Beck, P. K. Moitra & P. D'Arpa: Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin. J Biol Chem, 277, 40020-6 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 40020-40026
    • Rallabhandi, P.1    Hashimoto, K.2    Mo, Y.Y.3    Beck, W.T.4    Moitra, P.K.5    D'Arpa, P.6
  • 50
    • 0347361512 scopus 로고    scopus 로고
    • SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression
    • Dobreva, G., J. Dambacher & R. Grosschedl: SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression. Genes Dev, 17, 3048-61 (2003)
    • (2003) Genes Dev , vol.17 , pp. 3048-3061
    • Dobreva, G.1    Dambacher, J.2    Grosschedl, R.3
  • 51
    • 1942437991 scopus 로고    scopus 로고
    • SUMO: A regulator of gene expression and genome integrity
    • Muller, S., A. Ledl & D. Schmidt: SUMO: a regulator of gene expression and genome integrity. Oncogene, 23, 1998-2008 (2004)
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Muller, S.1    Ledl, A.2    Schmidt, D.3
  • 55
    • 0037163074 scopus 로고    scopus 로고
    • Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo
    • Eloranta, J. J. & H. C. Hurst: Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J Biol Chem, 277, 30798-804 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 30798-30804
    • Eloranta, J.J.1    Hurst, H.C.2
  • 57
    • 20344384269 scopus 로고    scopus 로고
    • SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin
    • Chalkiadaki, A. & I. Talianidis: SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin. Mol Cell Biol, 25, 5095-105 (2005)
    • (2005) Mol Cell Biol , vol.25 , pp. 5095-5105
    • Chalkiadaki, A.1    Talianidis, I.2
  • 58
    • 1542285164 scopus 로고    scopus 로고
    • SUMO promotes HDAC-mediated transcriptional repression
    • Yang, S. H. & A. D. Sharrocks: SUMO promotes HDAC-mediated transcriptional repression. Mol Cell, 13, 611-7 (2004)
    • (2004) Mol Cell , vol.13 , pp. 611-617
    • Yang, S.H.1    Sharrocks, A.D.2
  • 59
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio, Y. & R. N. Eisenman: Histone sumoylation is associated with transcriptional repression. Proc Natl Acad Sci U S A, 100, 13225-30 (2003)
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13225-13230
    • Shiio, Y.1    Eisenman, R.N.2
  • 61
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro, J. M., M. S. Rodriguez & R. T. Hay: SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell, 2, 233-9 (1998)
    • (1998) Mol Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 62
    • 0041731797 scopus 로고    scopus 로고
    • SUMO-1/Ubc9 promotes nuclear accumulation and metabolic stability of tumor suppressor Smad4
    • Lin, X., M. Liang, Y. Y. Liang, F. C. Brunicardi & X. H. Feng: SUMO-1/Ubc9 promotes nuclear accumulation and metabolic stability of tumor suppressor Smad4. J Biol Chem, 278, 31043-8 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 31043-31048
    • Lin, X.1    Liang, M.2    Liang, Y.Y.3    Brunicardi, F.C.4    Feng, X.H.5
  • 64
    • 3042693287 scopus 로고    scopus 로고
    • Increase of SUMO-1 expression in response to hypoxia: Direct interaction with HIF-1 alpha in adult mouse brain and heart in vivo
    • Shao, R., F. P. Zhang, F. Tian, P. Anders Friberg, X. Wang, H. Sjoland & H. Billig: Increase of SUMO-1 expression in response to hypoxia: direct interaction with HIF-1 alpha in adult mouse brain and heart in vivo. FEBS Lett, 569, 293-300 (2004)
    • (2004) FEBS Lett , vol.569 , pp. 293-300
    • Shao, R.1    Zhang, F.P.2    Tian, F.3    Anders Friberg, P.4    Wang, X.5    Sjoland, H.6    Billig, H.7
  • 66
    • 28844432700 scopus 로고    scopus 로고
    • SUMO recognition of a SUMO-binding motif: A reversal of the bound orientation
    • Song, J., Z. Zhang, W. Hu & Y. Chen: SUMO recognition of a SUMO-binding motif: A reversal of the bound orientation. J Biol Chem (2005)
    • (2005) J Biol Chem
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 67
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., B. Pfander, G. L. Moldovan, G. Pyrowolakis & S. Jentsch: RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature, 419, 135-41 (2002)
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 68
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter, P. & H. D. Ulrich: Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature, 425, 188-91 (2003)
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 69
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli, E., S. Chen, A. A. Davies, D. Huttner, L. Krejci, P. Sung & H. D. Ulrich: Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell, 19, 123-33 (2005)
    • (2005) Mol Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 70
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander, B., G. L. Moldovan, M. Sacher, C. Hoege & S. Jentsch: SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature, 436, 428-33 (2005)
    • (2005) Nature , vol.436 , pp. 428-433
    • Pfander, B.1    Moldovan, G.L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 71
    • 2942529467 scopus 로고    scopus 로고
    • Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae
    • Haracska, L., C. A. Torres-Ramos, R. E. Johnson, S. Prakash & L. Prakash: Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae. Mol Cell Biol, 24, 4267-74 (2004)
    • (2004) Mol Cell Biol , vol.24 , pp. 4267-4274
    • Haracska, L.1    Torres-Ramos, C.A.2    Johnson, R.E.3    Prakash, S.4    Prakash, L.5
  • 72
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche, P. L., J. Wing & A. R. Lehmann: Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol Cell, 14, 491-500 (2004)
    • (2004) Mol Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 73
    • 22244478319 scopus 로고    scopus 로고
    • DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation
    • Wang, Q. E., Q. Zhu, G. Wani, M. A. El-Mahdy, J. Li & A. A. Wani: DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Res, 33, 4023-34 (2005)
    • (2005) Nucleic Acids Res , vol.33 , pp. 4023-4034
    • Wang, Q.E.1    Zhu, Q.2    Wani, G.3    El-Mahdy, M.A.4    Li, J.5    Wani, A.A.6
  • 74
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe, K., S. Tateishi, M. Kawasuji, T. Tsurimoto, H. Inoue & M. Yamaizumi: Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. Embo J, 23, 3886-96 (2004)
    • (2004) Embo J , vol.23 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3    Tsurimoto, T.4    Inoue, H.5    Yamaizumi, M.6
  • 75
    • 0035799530 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of p53 modified by SUMO-1
    • Kwek, S. S., J. Deny, A. L. Tyner, Z. Shen & A. V. Gudkov: Functional analysis and intracellular localization of p53 modified by SUMO-1. Oncogene, 20, 2587-99 (2001)
    • (2001) Oncogene , vol.20 , pp. 2587-2599
    • Kwek, S.S.1    Deny, J.2    Tyner, A.L.3    Shen, Z.4    Gudkov, A.V.5
  • 76
    • 0037022564 scopus 로고    scopus 로고
    • Members of the PIAS family act as SUMO ligases for o-Jun and p53 and repress p53 activity
    • Schmidt, D. & S. Muller: Members of the PIAS family act as SUMO ligases for o-Jun and p53 and repress p53 activity. Proc Natl Acad Sci U S A, 99, 2872-7 (2002)
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2872-2877
    • Schmidt, D.1    Muller, S.2
  • 78
  • 79
    • 19844383887 scopus 로고    scopus 로고
    • Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor
    • Ledl, A., D. Schmidt & S. Muller: Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor. Oncogene, 24, 3810-8 (2005)
    • (2005) Oncogene , vol.24 , pp. 3810-3818
    • Ledl, A.1    Schmidt, D.2    Muller, S.3
  • 81
    • 16544362972 scopus 로고    scopus 로고
    • Differential PIAS3 expression in human malignancy
    • Wang, L. & S. Banerjee: Differential PIAS3 expression in human malignancy. Oncol Rep, 11, 1319-24 (2004)
    • (2004) Oncol Rep , vol.11 , pp. 1319-1324
    • Wang, L.1    Banerjee, S.2
  • 83
    • 3042758476 scopus 로고    scopus 로고
    • Ubiquitinated or sumoylated retinoic acid receptor alpha determines its characteristic and interacting model with retinoid X receptor alpha in gastric and breast cancer cells
    • Wu, Q., X. F. Lin, X. F. Ye, B. Zhang, Z. Xie & W. J. Su: Ubiquitinated or sumoylated retinoic acid receptor alpha determines its characteristic and interacting model with retinoid X receptor alpha in gastric and breast cancer cells. J Mol Endocrinol, 32, 595-613 (2004)
    • (2004) J Mol Endocrinol , vol.32 , pp. 595-613
    • Wu, Q.1    Lin, X.F.2    Ye, X.F.3    Zhang, B.4    Xie, Z.5    Su, W.J.6
  • 84
    • 16544390672 scopus 로고    scopus 로고
    • Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs
    • Mo, Y. Y., Y. Yu, P. L. Ee & W. T. Beck: Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs. Cancer Res, 64, 2793-8 (2004)
    • (2004) Cancer Res , vol.64 , pp. 2793-2798
    • Mo, Y.Y.1    Yu, Y.2    Ee, P.L.3    Beck, W.T.4
  • 85
    • 0032544309 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx
    • Chang, H. Y., H. Nishitoh, X. Yang, H. Ichijo & D. Baltimore: Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. Science, 281, 1860-3 (1998)
    • (1998) Science , vol.281 , pp. 1860-1863
    • Chang, H.Y.1    Nishitoh, H.2    Yang, X.3    Ichijo, H.4    Baltimore, D.5
  • 86
    • 0033119162 scopus 로고    scopus 로고
    • Coactivator and corepressor complexes in nuclear receptor function
    • Xu, L., C. K. Glass & M. G. Rosenfeld: Coactivator and corepressor complexes in nuclear receptor function. Curr Opin Genet Dev, 9, 140-7 (1999)
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 140-147
    • Xu, L.1    Glass, C.K.2    Rosenfeld, M.G.3
  • 87
    • 0037809267 scopus 로고    scopus 로고
    • Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1
    • Chauchereau, A., L. Amazit, M. Quesne, A. GuiochonMantel & E. Milgrom: Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1. J Biol Chem, 278, 12335-43 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 12335-12343
    • Chauchereau, A.1    Amazit, L.2    Quesne, M.3    GuiochonMantel, A.4    Milgrom, E.5
  • 88
    • 0036721526 scopus 로고    scopus 로고
    • Potentiation of glucocorticoid receptor transcriptional activity by sumoylation
    • Le Drean, Y., N. Mincheneau, P. Le Goff & D. Michel: Potentiation of glucocorticoid receptor transcriptional activity by sumoylation. Endocrinology, 143, 3482-9 (2002)
    • (2002) Endocrinology , vol.143 , pp. 3482-3489
    • Le Drean, Y.1    Mincheneau, N.2    Le Goff, P.3    Michel, D.4
  • 89
    • 0036826887 scopus 로고    scopus 로고
    • PIAS1 and PIASxalpha function as SUMOE3 ligases toward androgen receptor and repress androgen receptor-dependent transcription
    • Nishida, T. & H. Yasuda: PIAS1 and PIASxalpha function as SUMOE3 ligases toward androgen receptor and repress androgen receptor-dependent transcription. J Biol Chem, 211, 41311-7 (2002)
    • (2002) J Biol Chem , vol.211 , pp. 41311-41317
    • Nishida, T.1    Yasuda, H.2
  • 90
    • 3142716146 scopus 로고    scopus 로고
    • Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification
    • Ohshima, T., H. Koga & K. Shimotohno: Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification. J Biol Chem, 279, 29551-7 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 29551-29557
    • Ohshima, T.1    Koga, H.2    Shimotohno, K.3
  • 92
    • 0036645414 scopus 로고    scopus 로고
    • Molecular biology of the androgen receptor
    • Gelmann, E. P.: Molecular biology of the androgen receptor. J Clin Oncol, 20, 3001-15 (2002)
    • (2002) J Clin Oncol , vol.20 , pp. 3001-3015
    • Gelmann, E.P.1
  • 93
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna, N. J. & B. W. O'Malley: Combinatorial control of gene expression by nuclear receptors and coregulators. Cell, 108, 465-74 (2002)
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 94
    • 0036219918 scopus 로고    scopus 로고
    • Androgen receptor (AR) coregulators: An overview
    • Heinlein, C. A. & C. Chang: Androgen receptor (AR) coregulators: an overview. Endocr Rev, 23, 175-200 (2002)
    • (2002) Endocr Rev , vol.23 , pp. 175-200
    • Heinlein, C.A.1    Chang, C.2
  • 95
    • 0036208492 scopus 로고    scopus 로고
    • Formation of the androgen receptor transcription complex
    • Shang, Y., M. Myers & M. Brown: Formation of the androgen receptor transcription complex. Mol Cell, 9, 601-10 (2002)
    • (2002) Mol Cell , vol.9 , pp. 601-610
    • Shang, Y.1    Myers, M.2    Brown, M.3
  • 96
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H., U. Karvonen, O. A. Janne & J. J. Palvimo: Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc Natl Acad Sci U S A, 97, 14145-50 (2000)
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 97
    • 0033859780 scopus 로고    scopus 로고
    • A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy
    • Iniguez-Lluhi, J. A. & D. Pearce: A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy. Mol Cell Biol, 20, 6040-50 (2000)
    • (2000) Mol Cell Biol , vol.20 , pp. 6040-6050
    • Iniguez-Lluhi, J.A.1    Pearce, D.2
  • 98
    • 2542487192 scopus 로고    scopus 로고
    • Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements
    • Callewaert, L., G. Verrijdt, A. Haelens & F. Ciaessens: Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements. Mol Endocrinol, 18, 1438-49 (2004)
    • (2004) Mol Endocrinol , vol.18 , pp. 1438-1449
    • Callewaert, L.1    Verrijdt, G.2    Haelens, A.3    Ciaessens, F.4
  • 99
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass, C. K. & M. G. Rosenfeld: The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev, 14, 121-41 (2000)
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 100
    • 4143114765 scopus 로고    scopus 로고
    • Acetylation of nuclear receptors in cellular growth and apoptosis
    • Fu, M., C. Wang, X. Zhang & R. G. Pestell: Acetylation of nuclear receptors in cellular growth and apoptosis. Biochem Pharmacol, 68, 1199-208 (2004)
    • (2004) Biochem Pharmacol , vol.68 , pp. 1199-1208
    • Fu, M.1    Wang, C.2    Zhang, X.3    Pestell, R.G.4
  • 101
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • David, G., M. A. Neptune & R. A. DePinho: SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J Biol Chem, 277, 23658-63 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    DePinho, R.A.3
  • 102
    • 0037119457 scopus 로고    scopus 로고
    • The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1
    • Kotaja, N., U. Karvonen, O. A. Janne & J. J. Palvimo: The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1. J Biol Chem, 277, 30283-8 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 30283-30288
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 103
    • 0344874663 scopus 로고    scopus 로고
    • hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci
    • Sharma, M., X. Li, Y. Wang, M. Zarnegar, C. Y. Huang, J. J. Palvimo, B. Lim & Z. Sun: hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci. Embo J, 22, 6101-14 (2003)
    • (2003) Embo J , vol.22 , pp. 6101-6114
    • Sharma, M.1    Li, X.2    Wang, Y.3    Zarnegar, M.4    Huang, C.Y.5    Palvimo, J.J.6    Lim, B.7    Sun, Z.8
  • 104
    • 2942735131 scopus 로고    scopus 로고
    • SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1
    • Cheng, J., D. Wang, Z. Wang & E. T. Yeh: SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol Cell Biol, 24, 6021-8 (2004)
    • (2004) Mol Cell Biol , vol.24 , pp. 6021-6028
    • Cheng, J.1    Wang, D.2    Wang, Z.3    Yeh, E.T.4
  • 105
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • Bies, J., J. Markus & L. Wolff: Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J Biol Chem, 277, 8999-9009 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 106
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang, Y., X. Hu, J. DiRenzo, M. A. Lazar & M. Brown: Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell, 103, 843-52 (2000)
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 107
    • 0035963311 scopus 로고    scopus 로고
    • Distinct effects of PIAS proteins on androgenmediated gene activation in prostate cancer cells
    • Gross, M., B. Liu, J. Tan, F. S. French, M. Carey & K. Shuai: Distinct effects of PIAS proteins on androgenmediated gene activation in prostate cancer cells. Oncogene, 20, 3880-7 (2001)
    • (2001) Oncogene , vol.20 , pp. 3880-3887
    • Gross, M.1    Liu, B.2    Tan, J.3    French, F.S.4    Carey, M.5    Shuai, K.6
  • 108
    • 2442484492 scopus 로고    scopus 로고
    • PIASy-mediated repression of the androgen receptor is independent of sumoylation
    • Gross, M., R. Yang, I. Top, C. Gasper & K. Shuai: PIASy-mediated repression of the androgen receptor is independent of sumoylation. Oncogene, 23, 3059-66 (2004)
    • (2004) Oncogene , vol.23 , pp. 3059-3066
    • Gross, M.1    Yang, R.2    Top, I.3    Gasper, C.4    Shuai, K.5
  • 110
    • 0035930133 scopus 로고    scopus 로고
    • Androgen receptor signaling in androgen-refractory prostate cancer
    • Grossmann, M. E., H. Huang & D. J. Tindall: Androgen receptor signaling in androgen-refractory prostate cancer. J Natl Cancer Inst, 93, 1687-97 (2001)
    • (2001) J Natl Cancer Inst , vol.93 , pp. 1687-1697
    • Grossmann, M.E.1    Huang, H.2    Tindall, D.J.3
  • 111
    • 0036791444 scopus 로고    scopus 로고
    • Heterogeneous expression and functions of androgen receptor co-factors in primary prostate cancer
    • Li, P., X. Yu, K. Ge, J. Melamed, R. G. Roeder & Z. Wang: Heterogeneous expression and functions of androgen receptor co-factors in primary prostate cancer. Am J Pathol, 161, 1467-74 (2002)
    • (2002) Am J Pathol , vol.161 , pp. 1467-1474
    • Li, P.1    Yu, X.2    Ge, K.3    Melamed, J.4    Roeder, R.G.5    Wang, Z.6
  • 114
    • 28844506843 scopus 로고    scopus 로고
    • SUMOylation of the Estrogen receptor {alpha} hinge region by SUMO-E3 ligases PIAS1 and PIAS3 regulates ER {alpha} transcriptional activity
    • Sentis, S., M. Le Romancer, C. Bianchin, M. C. Rostan & L. Corbo: SUMOylation of the Estrogen receptor {alpha} hinge region by SUMO-E3 ligases PIAS1 and PIAS3 regulates ER {alpha} transcriptional activity. Mol Endocrinol (2005)
    • (2005) Mol Endocrinol
    • Sentis, S.1    Le Romancer, M.2    Bianchin, C.3    Rostan, M.C.4    Corbo, L.5
  • 115
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • Leo, C. & J. D. Chen: The SRC family of nuclear receptor coactivators. Gene, 245, 1-11 (2000)
    • (2000) Gene , vol.245 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 118
    • 0033120030 scopus 로고    scopus 로고
    • Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1
    • Tremblay, A., G. B. Tremblay, F. Labrie & V. Giguere: Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1. Mol Cell, 3, 513-9 (1999)
    • (1999) Mol Cell , vol.3 , pp. 513-519
    • Tremblay, A.1    Tremblay, G.B.2    Labrie, F.3    Giguere, V.4


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