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Volumn 6, Issue 10, 2011, Pages

Sumoylation of the forkhead transcription factor FOXL2 promotes its stabilization/activation through transient recruitment to PML bodies

Author keywords

[No Author keywords available]

Indexed keywords

FORKHEAD TRANSCRIPTION FACTOR; NUCLEAR FACTOR; PROTEIN FOXL2; UNCLASSIFIED DRUG; FOXL2 PROTEIN, HUMAN; MUTANT PROTEIN; PEPTIDE;

EID: 80053945453     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025463     Document Type: Article
Times cited : (22)

References (65)
  • 3
    • 0035131812 scopus 로고    scopus 로고
    • The putative forkhead transcription factor FOXL2 is mutated in blepharophimosis/ptosis/epicanthus inversus syndrome
    • Crisponi L, Deiana M, Loi A, Chiappe F, Uda M, et al. (2001) The putative forkhead transcription factor FOXL2 is mutated in blepharophimosis/ptosis/epicanthus inversus syndrome. Nat Genet 27: 159-166.
    • (2001) Nat Genet , vol.27 , pp. 159-166
    • Crisponi, L.1    Deiana, M.2    Loi, A.3    Chiappe, F.4    Uda, M.5
  • 4
    • 0020508397 scopus 로고
    • The blepharophimosis, ptosis, and epicanthus inversus syndrome: delineation of two types
    • Zlotogora J, Sagi M, Cohen T, (1983) The blepharophimosis, ptosis, and epicanthus inversus syndrome: delineation of two types. Am J Hum Genet 35: 1020-1027.
    • (1983) Am J Hum Genet , vol.35 , pp. 1020-1027
    • Zlotogora, J.1    Sagi, M.2    Cohen, T.3
  • 5
    • 0036061053 scopus 로고    scopus 로고
    • Identification of novel mutations in FOXL2 associated with premature ovarian failure
    • Harris SE, Chand AL, Winship IM, Gersak K, Aittomäki K, et al. (2002) Identification of novel mutations in FOXL2 associated with premature ovarian failure. Mol Hum Reprod 8: 729-733.
    • (2002) Mol Hum Reprod , vol.8 , pp. 729-733
    • Harris, S.E.1    Chand, A.L.2    Winship, I.M.3    Gersak, K.4    Aittomäki, K.5
  • 6
    • 67650508076 scopus 로고    scopus 로고
    • Functional evidence implicating FOXL2 in non-syndromic premature ovarian failure and in the regulation of the transcription factor OSR2
    • Laissue P, Lakhal B, Benayoun BA, Dipietromaria A, Braham R, et al. (2009) Functional evidence implicating FOXL2 in non-syndromic premature ovarian failure and in the regulation of the transcription factor OSR2. J Med Genet 46: 455-457.
    • (2009) J Med Genet , vol.46 , pp. 455-457
    • Laissue, P.1    Lakhal, B.2    Benayoun, B.A.3    Dipietromaria, A.4    Braham, R.5
  • 7
    • 71149095052 scopus 로고    scopus 로고
    • Somatic Sex Reprogramming of Adult Ovaries to Testes by FOXL2 Ablation
    • Uhlenhaut NH, Jakob S, Anlag K, Eisenberger T, Sekido R, et al. (2009) Somatic Sex Reprogramming of Adult Ovaries to Testes by FOXL2 Ablation. Cell 139: 1130-1142.
    • (2009) Cell , vol.139 , pp. 1130-1142
    • Uhlenhaut, N.H.1    Jakob, S.2    Anlag, K.3    Eisenberger, T.4    Sekido, R.5
  • 8
    • 35748965278 scopus 로고    scopus 로고
    • Loss of Wnt4 and Foxl2 leads to female-to-male sex reversal extending to germ cells
    • Ottolenghi C, Pelosi E, Tran J, Colombino M, Douglass E, et al. (2007) Loss of Wnt4 and Foxl2 leads to female-to-male sex reversal extending to germ cells. Hum Mol Genet 16: 2795-2804.
    • (2007) Hum Mol Genet , vol.16 , pp. 2795-2804
    • Ottolenghi, C.1    Pelosi, E.2    Tran, J.3    Colombino, M.4    Douglass, E.5
  • 9
    • 1342327343 scopus 로고    scopus 로고
    • The murine winged-helix transcription factor Foxl2 is required for granulosa cell differentiation and ovary maintenance
    • Schmidt D, Ovitt CE, Anlag K, Fehsenfeld S, Gredsted L, et al. (2004) The murine winged-helix transcription factor Foxl2 is required for granulosa cell differentiation and ovary maintenance. Development 131: 933-942.
    • (2004) Development , vol.131 , pp. 933-942
    • Schmidt, D.1    Ovitt, C.E.2    Anlag, K.3    Fehsenfeld, S.4    Gredsted, L.5
  • 10
    • 67649406102 scopus 로고    scopus 로고
    • Mutation of FOXL2 in granulosa-cell tumors of the ovary
    • Shah SP, Köbel M, Senz J, Morin RD, Clarke BA, et al. (2009) Mutation of FOXL2 in granulosa-cell tumors of the ovary. N Engl J Med 360: 2719-2729.
    • (2009) N Engl J Med , vol.360 , pp. 2719-2729
    • Shah, S.P.1    Köbel, M.2    Senz, J.3    Morin, R.D.4    Clarke, B.A.5
  • 11
    • 33847666428 scopus 로고    scopus 로고
    • Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics
    • Batista F, Vaiman D, Dausset J, Fellous M, Veitia RA, (2007) Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics. Proc Natl Acad Sci U S A 104: 3330-3335.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3330-3335
    • Batista, F.1    Vaiman, D.2    Dausset, J.3    Fellous, M.4    Veitia, R.A.5
  • 12
    • 58949102956 scopus 로고    scopus 로고
    • Positive and negative feedback regulates the transcription factor FOXL2 in response to cell stress: evidence for a regulatory imbalance induced by disease-causing mutations
    • Benayoun BA, Batista F, Auer J, Dipietromaria A, L'Hôte D, et al. (2009) Positive and negative feedback regulates the transcription factor FOXL2 in response to cell stress: evidence for a regulatory imbalance induced by disease-causing mutations. Hum Mol Genet 18: 632-644.
    • (2009) Hum Mol Genet , vol.18 , pp. 632-644
    • Benayoun, B.A.1    Batista, F.2    Auer, J.3    Dipietromaria, A.4    L'Hôte, D.5
  • 13
    • 25144456097 scopus 로고    scopus 로고
    • Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis
    • Lee K, Pisarska MD, Ko J-J, Kang Y, Yoon S, et al. (2005) Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis. Biochem Biophys Res Commun 336: 876-881.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 876-881
    • Lee, K.1    Pisarska, M.D.2    Ko, J.-J.3    Kang, Y.4    Yoon, S.5
  • 14
    • 77953468513 scopus 로고    scopus 로고
    • Microarray analysis of Foxl2 mediated gene regulation in the mouse ovary derived KK1 granulosa cell line: Over-expression of Foxl2 leads to activation of the gonadotropin releasing hormone receptor gene promoter
    • Escudero JM, Haller JL, Clay CM, Escudero KW, (2010) Microarray analysis of Foxl2 mediated gene regulation in the mouse ovary derived KK1 granulosa cell line: Over-expression of Foxl2 leads to activation of the gonadotropin releasing hormone receptor gene promoter. J Ovarian Res 3: 4.
    • (2010) J Ovarian Res , vol.3 , pp. 4
    • Escudero, J.M.1    Haller, J.L.2    Clay, C.M.3    Escudero, K.W.4
  • 16
    • 70349783734 scopus 로고    scopus 로고
    • Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the Steroidogenic Acute Regulatory gene
    • Kuo F-T, Bentsi-Barnes IK, Barlow GM, Bae J, Pisarska MD, (2009) Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the Steroidogenic Acute Regulatory gene. Cell Signal 21: 1935-1944.
    • (2009) Cell Signal , vol.21 , pp. 1935-1944
    • Kuo, F.-T.1    Bentsi-Barnes, I.K.2    Barlow, G.M.3    Bae, J.4    Pisarska, M.D.5
  • 17
    • 77949720991 scopus 로고    scopus 로고
    • The forkhead transcription factor Foxl2 is sumoylated in both human and mouse: sumoylation affects its stability, localization, and activity
    • Marongiu M, Deiana M, Meloni A, Marcia L, Puddu A, et al. (2010) The forkhead transcription factor Foxl2 is sumoylated in both human and mouse: sumoylation affects its stability, localization, and activity. PLoS ONE 5: e9477.
    • (2010) PLoS ONE , vol.5
    • Marongiu, M.1    Deiana, M.2    Meloni, A.3    Marcia, L.4    Puddu, A.5
  • 18
    • 79953169851 scopus 로고    scopus 로고
    • Minireview: Roles of the Forkhead Transcription Factor FOXL2 in Granulosa Cell Biology and Pathology
    • Pisarska MD, Barlow G, Kuo F-T, (2011) Minireview: Roles of the Forkhead Transcription Factor FOXL2 in Granulosa Cell Biology and Pathology. Endocrinology 152: 1199-1208.
    • (2011) Endocrinology , vol.152 , pp. 1199-1208
    • Pisarska, M.D.1    Barlow, G.2    Kuo, F.-T.3
  • 19
    • 65149105339 scopus 로고    scopus 로고
    • A post-translational modification code for transcription factors: sorting through a sea of signals
    • Benayoun BA, Veitia RA, (2009) A post-translational modification code for transcription factors: sorting through a sea of signals. Trends Cell Biol 19: 189-197.
    • (2009) Trends Cell Biol , vol.19 , pp. 189-197
    • Benayoun, B.A.1    Veitia, R.A.2
  • 20
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson ES, (2004) Protein modification by SUMO. Annu Rev Biochem 73: 355-382.
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 21
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M, (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 23
    • 15944406765 scopus 로고    scopus 로고
    • SUMOA History of Modification
    • Hay RT, (2005) SUMOA History of Modification. Molecular Cell 18: 1-12.
    • (2005) Molecular Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 25
    • 40849150778 scopus 로고    scopus 로고
    • Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen
    • Stielow B, Sapetschnig A, Krüger I, Kunert N, Brehm A, et al. (2008) Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen. Mol Cell 29: 742-754.
    • (2008) Mol Cell , vol.29 , pp. 742-754
    • Stielow, B.1    Sapetschnig, A.2    Krüger, I.3    Kunert, N.4    Brehm, A.5
  • 26
    • 0035955662 scopus 로고    scopus 로고
    • Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification
    • Hong Y, Rogers R, Matunis MJ, Mayhew CN, Goodson ML, et al. (2001) Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification. J Biol Chem 276: 40263-40267.
    • (2001) J Biol Chem , vol.276 , pp. 40263-40267
    • Hong, Y.1    Rogers, R.2    Matunis, M.J.3    Mayhew, C.N.4    Goodson, M.L.5
  • 27
    • 0035947677 scopus 로고    scopus 로고
    • Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor
    • Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, et al. (2001) Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor. J Biol Chem 276: 18513-18518.
    • (2001) J Biol Chem , vol.276 , pp. 18513-18518
    • Goodson, M.L.1    Hong, Y.2    Rogers, R.3    Matunis, M.J.4    Park-Sarge, O.K.5
  • 28
    • 3142544806 scopus 로고    scopus 로고
    • Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1
    • Terui Y, Saad N, Jia S, McKeon F, Yuan J, (2004) Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1. J Biol Chem 279: 28257-28265.
    • (2004) J Biol Chem , vol.279 , pp. 28257-28265
    • Terui, Y.1    Saad, N.2    Jia, S.3    McKeon, F.4    Yuan, J.5
  • 29
    • 33744915576 scopus 로고    scopus 로고
    • Interactions between PIAS proteins and SOX9 result in an increase in the cellular concentrations of SOX9
    • Hattori T, Eberspaecher H, Lu J, Zhang R, Nishida T, et al. (2006) Interactions between PIAS proteins and SOX9 result in an increase in the cellular concentrations of SOX9. J Biol Chem 281: 14417-14428.
    • (2006) J Biol Chem , vol.281 , pp. 14417-14428
    • Hattori, T.1    Eberspaecher, H.2    Lu, J.3    Zhang, R.4    Nishida, T.5
  • 30
    • 44449090072 scopus 로고    scopus 로고
    • SUMOylation regulates the transcriptional activity of JunB in T lymphocytes
    • Garaude J, Farrás R, Bossis G, Charni S, Piechaczyk M, et al. (2008) SUMOylation regulates the transcriptional activity of JunB in T lymphocytes. J Immunol 180: 5983-5990.
    • (2008) J Immunol , vol.180 , pp. 5983-5990
    • Garaude, J.1    Farrás, R.2    Bossis, G.3    Charni, S.4    Piechaczyk, M.5
  • 31
  • 32
    • 63849135038 scopus 로고    scopus 로고
    • PML nuclear bodies and their spatial relationships in the mammalian cell nucleus
    • Batty E, Jensen K, Freemont P, (2009) PML nuclear bodies and their spatial relationships in the mammalian cell nucleus. Front Biosci 14: 1182-1196.
    • (2009) Front Biosci , vol.14 , pp. 1182-1196
    • Batty, E.1    Jensen, K.2    Freemont, P.3
  • 33
    • 76649083577 scopus 로고    scopus 로고
    • Three-dimensional organization of promyelocytic leukemia nuclear bodies
    • Lang M, Jegou T, Chung I, Richter K, Münch S, et al. (2010) Three-dimensional organization of promyelocytic leukemia nuclear bodies. J Cell Sci 123: 392-400.
    • (2010) J Cell Sci , vol.123 , pp. 392-400
    • Lang, M.1    Jegou, T.2    Chung, I.3    Richter, K.4    Münch, S.5
  • 34
    • 77449089538 scopus 로고    scopus 로고
    • A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
    • Van Damme E, Laukens K, Dang TH, Van Ostade X, (2010) A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics. Int J Biol Sci 6: 51-67.
    • (2010) Int J Biol Sci , vol.6 , pp. 51-67
    • van Damme, E.1    Laukens, K.2    Dang, T.H.3    van Ostade, X.4
  • 35
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • Negorev D, Maul GG, (2001) Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 20: 7234-7242.
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 38
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R, Pandolfi PP, (2007) Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nature Reviews Molecular Cell Biology 8: 1006-1016.
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 39
    • 3042554114 scopus 로고    scopus 로고
    • Forkhead l2 is expressed in the ovary and represses the promoter activity of the steroidogenic acute regulatory gene
    • Pisarska MD, Bae J, Klein C, Hsueh AJW, (2004) Forkhead l2 is expressed in the ovary and represses the promoter activity of the steroidogenic acute regulatory gene. Endocrinology 145: 3424-3433.
    • (2004) Endocrinology , vol.145 , pp. 3424-3433
    • Pisarska, M.D.1    Bae, J.2    Klein, C.3    Hsueh, A.J.W.4
  • 40
    • 17744364049 scopus 로고    scopus 로고
    • Establishment and characterization of a steroidogenic human granulosa-like tumor cell line, KGN, that expresses functional follicle-stimulating hormone receptor
    • Nishi Y, Yanase T, Mu Y, Oba K, Ichino I, et al. (2001) Establishment and characterization of a steroidogenic human granulosa-like tumor cell line, KGN, that expresses functional follicle-stimulating hormone receptor. Endocrinology 142: 437-445.
    • (2001) Endocrinology , vol.142 , pp. 437-445
    • Nishi, Y.1    Yanase, T.2    Mu, Y.3    Oba, K.4    Ichino, I.5
  • 41
    • 16544390672 scopus 로고    scopus 로고
    • Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs
    • Mo Y-Y, Yu Y, Ee PLR, Beck WT, (2004) Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs. Cancer Res 64: 2793-2798.
    • (2004) Cancer Res , vol.64 , pp. 2793-2798
    • Mo, Y.-Y.1    Yu, Y.2    Ee, P.L.R.3    Beck, W.T.4
  • 42
    • 79954545155 scopus 로고    scopus 로고
    • Transcription factor FOXL2 protects granulosa cells from stress and delays cell cycle: role of its regulation by the SIRT1 deacetylase
    • May
    • Benayoun BA, Georges AB, L'hôte D, Andersson N, Dipietromaria A, et al. (2011) Transcription factor FOXL2 protects granulosa cells from stress and delays cell cycle: role of its regulation by the SIRT1 deacetylase. Hum Mol Genet 2011 May 1;20 (9): 1673-86.
    • (2011) Hum Mol Genet , vol.2011 , Issue.9 , pp. 1673-1686
    • Benayoun, B.A.1    Georges, A.B.2    L'hôte, D.3    Andersson, N.4    Dipietromaria, A.5
  • 43
    • 18044364791 scopus 로고    scopus 로고
    • Mechanism of the tumor suppressive effect of MnSOD overexpression
    • Oberley LW, (2005) Mechanism of the tumor suppressive effect of MnSOD overexpression. Biomed Pharmacother 59: 143-148.
    • (2005) Biomed Pharmacother , vol.59 , pp. 143-148
    • Oberley, L.W.1
  • 44
    • 33645519583 scopus 로고    scopus 로고
    • Tumor suppression by the mammalian Period genes
    • Lee CC, (2006) Tumor suppression by the mammalian Period genes. Cancer Causes Control 17: 525-530.
    • (2006) Cancer Causes Control , vol.17 , pp. 525-530
    • Lee, C.C.1
  • 45
    • 45749152585 scopus 로고    scopus 로고
    • Missense mutations in the forkhead domain of FOXL2 lead to subcellular mislocalization, protein aggregation and impaired transactivation
    • Beysen D, Moumné L, Veitia R, Peters H, Leroy BP, et al. (2008) Missense mutations in the forkhead domain of FOXL2 lead to subcellular mislocalization, protein aggregation and impaired transactivation. Hum Mol Genet 17: 2030-2038.
    • (2008) Hum Mol Genet , vol.17 , pp. 2030-2038
    • Beysen, D.1    Moumné, L.2    Veitia, R.3    Peters, H.4    Leroy, B.P.5
  • 46
    • 10844222804 scopus 로고    scopus 로고
    • A recurrent polyalanine expansion in the transcription factor FOXL2 induces extensive nuclear and cytoplasmic protein aggregation
    • Caburet S, Demarez A, Moumné L, Fellous M, De Baere E, et al. (2004) A recurrent polyalanine expansion in the transcription factor FOXL2 induces extensive nuclear and cytoplasmic protein aggregation. J Med Genet 41: 932-936.
    • (2004) J Med Genet , vol.41 , pp. 932-936
    • Caburet, S.1    Demarez, A.2    Moumné, L.3    Fellous, M.4    de Baere, E.5
  • 47
    • 41149124043 scopus 로고    scopus 로고
    • Differential aggregation and functional impairment induced by polyalanine expansions in FOXL2, a transcription factor involved in cranio-facial and ovarian development
    • Moumné L, Dipietromaria A, Batista F, Kocer A, Fellous M, et al. (2008) Differential aggregation and functional impairment induced by polyalanine expansions in FOXL2, a transcription factor involved in cranio-facial and ovarian development. Hum Mol Genet 17: 1010-1019.
    • (2008) Hum Mol Genet , vol.17 , pp. 1010-1019
    • Moumné, L.1    Dipietromaria, A.2    Batista, F.3    Kocer, A.4    Fellous, M.5
  • 48
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: a model for nuclear organelles
    • Lamond AI, Spector DL, (2003) Nuclear speckles: a model for nuclear organelles. Nat Rev Mol Cell Biol 4: 605-612.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 49
    • 53449084759 scopus 로고    scopus 로고
    • The Cajal body
    • Morris GE, (2008) The Cajal body. Biochim Biophys Acta 1783: 2108-2115.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 2108-2115
    • Morris, G.E.1
  • 50
    • 67649766870 scopus 로고    scopus 로고
    • Transcription factories: gene expression in unions?
    • Sutherland H, Bickmore WA, (2009) Transcription factories: gene expression in unions? Nat Rev Genet 10: 457-466.
    • (2009) Nat Rev Genet , vol.10 , pp. 457-466
    • Sutherland, H.1    Bickmore, W.A.2
  • 51
  • 52
    • 0036796816 scopus 로고    scopus 로고
    • Sulfonation and Molecular Action
    • Strott CA, (2002) Sulfonation and Molecular Action. Endocrine Reviews 23: 703-732.
    • (2002) Endocrine Reviews , vol.23 , pp. 703-732
    • Strott, C.A.1
  • 54
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy
    • Xue Y, Ren J, Gao X, Jin C, Wen L, et al. (2008) GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy. Mol Cell Proteomics 7: 1598-1608.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1598-1608
    • Xue, Y.1    Ren, J.2    Gao, X.3    Jin, C.4    Wen, L.5
  • 55
    • 3343024236 scopus 로고    scopus 로고
    • Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha
    • Kannan N, Neuwald AF, (2004) Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha. Protein Sci 13: 2059-2077.
    • (2004) Protein Sci , vol.13 , pp. 2059-2077
    • Kannan, N.1    Neuwald, A.F.2
  • 56
    • 0032954260 scopus 로고    scopus 로고
    • Human homologue of the Drosophila melanogaster lats tumour suppressor modulates CDC2 activity
    • Tao W, Zhang S, Turenchalk GS, Stewart RA, St John MA, et al. (1999) Human homologue of the Drosophila melanogaster lats tumour suppressor modulates CDC2 activity. Nat Genet 21: 177-181.
    • (1999) Nat Genet , vol.21 , pp. 177-181
    • Tao, W.1    Zhang, S.2    Turenchalk, G.S.3    Stewart, R.A.4    St John, M.A.5
  • 57
    • 4143080721 scopus 로고    scopus 로고
    • Genetic analysis of a five generation Indian family with BPES: a novel missense mutation (p. Y215C)
    • Kumar A, Babu M, Raghunath A, Venkatesh CP, (2004) Genetic analysis of a five generation Indian family with BPES: a novel missense mutation (p. Y215C). Mol Vis 10: 445-449.
    • (2004) Mol Vis , vol.10 , pp. 445-449
    • Kumar, A.1    Babu, M.2    Raghunath, A.3    Venkatesh, C.P.4
  • 59
    • 66149103721 scopus 로고    scopus 로고
    • Sulfonation and Phosphorylation of Regions of the Dioxin Receptor Susceptible to Methionine Modifications
    • Dave KA, Whelan F, Bindloss C, Furness SGB, Chapman-Smith A, et al. (2009) Sulfonation and Phosphorylation of Regions of the Dioxin Receptor Susceptible to Methionine Modifications. Mol Cell Proteomics 8: 706-719.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 706-719
    • Dave, K.A.1    Whelan, F.2    Bindloss, C.3    Furness, S.G.B.4    Chapman-Smith, A.5
  • 60
    • 0035823497 scopus 로고    scopus 로고
    • Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
    • Thompson PR, Kurooka H, Nakatani Y, Cole PA, (2001) Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity. J Biol Chem 276: 33721-33729.
    • (2001) J Biol Chem , vol.276 , pp. 33721-33729
    • Thompson, P.R.1    Kurooka, H.2    Nakatani, Y.3    Cole, P.A.4
  • 61
    • 0033601328 scopus 로고    scopus 로고
    • Transcriptional activation of the human manganese superoxide dismutase gene mediated by tetradecanoylphorbol acetate
    • Kim HP, Roe JH, Chock PB, Yim MB, (1999) Transcriptional activation of the human manganese superoxide dismutase gene mediated by tetradecanoylphorbol acetate. J Biol Chem 274: 37455-37460.
    • (1999) J Biol Chem , vol.274 , pp. 37455-37460
    • Kim, H.P.1    Roe, J.H.2    Chock, P.B.3    Yim, M.B.4
  • 62
    • 20044396172 scopus 로고    scopus 로고
    • A noncanonical E-box enhancer drives mouse Period2 circadian oscillations in vivo
    • Yoo S-H, Ko CH, Lowrey PL, Buhr ED, Song E-joo, et al. (2005) A noncanonical E-box enhancer drives mouse Period2 circadian oscillations in vivo. Proc Natl Acad Sci U S A 102: 2608-2613.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2608-2613
    • Yoo, S.-H.1    Ko, C.H.2    Lowrey, P.L.3    Buhr, E.D.4    Song, E-J.5
  • 63
    • 33745046562 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2
    • Itahana Y, Yeh ETH, Zhang Y, (2006) Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2. Mol Cell Biol 26: 4675-4689.
    • (2006) Mol Cell Biol , vol.26 , pp. 4675-4689
    • Itahana, Y.1    Yeh, E.T.H.2    Zhang, Y.3
  • 64
    • 33745612063 scopus 로고    scopus 로고
    • PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins
    • Janer A, Martin E, Muriel M-P, Latouche M, Fujigasaki H, et al. (2006) PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins. J Cell Biol 174: 65-76.
    • (2006) J Cell Biol , vol.174 , pp. 65-76
    • Janer, A.1    Martin, E.2    Muriel, M.-P.3    Latouche, M.4    Fujigasaki, H.5


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