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Volumn 22, Issue 1, 2014, Pages 35-46

Structural insights into the recruitment of SMRT by the corepressor SHARP under phosphorylative regulation

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; HISTONE DEACETYLASE 1 ASSOCIATED REPRESSOR PROTEIN; PROTEIN; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; UNCLASSIFIED DRUG; COREPRESSOR PROTEIN; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR HDAC1 ASSOCIATED REPRESSOR PROTEIN;

EID: 84891886338     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.10.007     Document Type: Article
Times cited : (23)

References (51)
  • 1
    • 0001654819 scopus 로고
    • An alternative 3D NMR technique for correlating backbone 15N with side-chain Hb resonances in larger proteins
    • S.J. Archer, M. Ikura, D.A. Torchia, and A. Bax An alternative 3D NMR technique for correlating backbone 15N with side-chain Hb resonances in larger proteins J. Magn. Reson. 95 1991 636 641
    • (1991) J. Magn. Reson. , vol.95 , pp. 636-641
    • Archer, S.J.1    Ikura, M.2    Torchia, D.A.3    Bax, A.4
  • 2
    • 0042626227 scopus 로고    scopus 로고
    • A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling
    • M. Ariyoshi, and J.W. Schwabe A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling Genes Dev. 17 2003 1909 1920
    • (2003) Genes Dev. , vol.17 , pp. 1909-1920
    • Ariyoshi, M.1    Schwabe, J.W.2
  • 5
    • 16644402765 scopus 로고    scopus 로고
    • Effects of phosphorylation by protein kinase CK2 on the human basal components of the RNA polymerase II transcription machinery
    • M.E. Cabrejos, C.C. Allende, and E. Maldonado Effects of phosphorylation by protein kinase CK2 on the human basal components of the RNA polymerase II transcription machinery J. Cell. Biochem. 93 2004 2 10
    • (2004) J. Cell. Biochem. , vol.93 , pp. 2-10
    • Cabrejos, M.E.1    Allende, C.C.2    Maldonado, E.3
  • 7
    • 80053576647 scopus 로고    scopus 로고
    • Steroid receptor RNA activator - A nuclear receptor coregulator with multiple partners: Insights and challenges
    • S.M. Colley, and P.J. Leedman Steroid receptor RNA activator - a nuclear receptor coregulator with multiple partners: insights and challenges Biochimie 93 2011 1966 1972
    • (2011) Biochimie , vol.93 , pp. 1966-1972
    • Colley, S.M.1    Leedman, P.J.2
  • 8
    • 80053572392 scopus 로고    scopus 로고
    • Steroid receptor RNA activator bi-faceted genetic system: Heads or tails?
    • C. Cooper, D. Vincett, Y. Yan, M.K. Hamedani, Y. Myal, and E. Leygue Steroid receptor RNA activator bi-faceted genetic system: heads or tails? Biochimie 93 2011 1973 1980
    • (2011) Biochimie , vol.93 , pp. 1973-1980
    • Cooper, C.1    Vincett, D.2    Yan, Y.3    Hamedani, M.K.4    Myal, Y.5    Leygue, E.6
  • 9
    • 27644545507 scopus 로고    scopus 로고
    • An AMBER/DYANA/MOLMOL phosphorylated amino acid library set and incorporation into NMR structure calculations
    • J.W. Craft Jr., and G.B. Legge An AMBER/DYANA/MOLMOL phosphorylated amino acid library set and incorporation into NMR structure calculations J. Biomol. NMR 33 2005 15 24
    • (2005) J. Biomol. NMR , vol.33 , pp. 15-24
    • Craft, Jr.J.W.1    Legge, G.B.2
  • 10
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • J.E. Darnell Jr., I.M. Kerr, and G.R. Stark Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins Science 264 1994 1415 1421
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, Jr.J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 13
    • 0037085684 scopus 로고    scopus 로고
    • P65-NFkappaB synergizes with Notch to activate transcription by triggering cytoplasmic translocation of the nuclear receptor corepressor N-CoR
    • L. Espinosa, S. Santos, J. Inglés-Esteve, P. Muñoz-Canoves, and A. Bigas p65-NFkappaB synergizes with Notch to activate transcription by triggering cytoplasmic translocation of the nuclear receptor corepressor N-CoR J. Cell Sci. 115 2002 1295 1303
    • (2002) J. Cell Sci. , vol.115 , pp. 1295-1303
    • Espinosa, L.1    Santos, S.2    Inglés-Esteve, J.3    Muñoz-Canoves, P.4    Bigas, A.5
  • 14
    • 6344287454 scopus 로고    scopus 로고
    • Interactions between BRCT repeats and phosphoproteins: Tangled up in two
    • J.N. Glover, R.S. Williams, and M.S. Lee Interactions between BRCT repeats and phosphoproteins: tangled up in two Trends Biochem. Sci. 29 2004 579 585
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 579-585
    • Glover, J.N.1    Williams, R.S.2    Lee, M.S.3
  • 15
    • 0001682998 scopus 로고
    • A 3D triple-resonance NMR technique for qualitative measurement of carbonyl-Hb J coplings in isotopically enriched protein
    • S. Grzesiek, M. Ikura, G.M. Clore, A.M. Gronenborn, and A. Bax A 3D triple-resonance NMR technique for qualitative measurement of carbonyl-Hb J coplings in isotopically enriched protein J. Magn. Reson. 96 1992 215 221
    • (1992) J. Magn. Reson. , vol.96 , pp. 215-221
    • Grzesiek, S.1    Ikura, M.2    Clore, G.M.3    Gronenborn, A.M.4    Bax, A.5
  • 16
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-cyclin e complex: Multisite-phosphorylated substrate recognition by SCF ubiquitin ligases
    • B. Hao, S. Oehlmann, M.E. Sowa, J.W. Harper, and N.P. Pavletich Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases Mol. Cell 26 2007 131 143
    • (2007) Mol. Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 17
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Güntert, and K. Wüthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 18
    • 0037197893 scopus 로고    scopus 로고
    • Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein
    • M.K. Homma, D. Li, E.G. Krebs, Y. Yuasa, and Y. Homma Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein Proc. Natl. Acad. Sci. USA 99 2002 5959 5964
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5959-5964
    • Homma, M.K.1    Li, D.2    Krebs, E.G.3    Yuasa, Y.4    Homma, Y.5
  • 19
    • 27344436940 scopus 로고    scopus 로고
    • CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cycle progression
    • M.K. Homma, I. Wada, T. Suzuki, J. Yamaki, E.G. Krebs, and Y. Homma CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cycle progression Proc. Natl. Acad. Sci. USA 102 2005 15688 15693
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15688-15693
    • Homma, M.K.1    Wada, I.2    Suzuki, T.3    Yamaki, J.4    Krebs, E.G.5    Homma, Y.6
  • 20
    • 0033838465 scopus 로고    scopus 로고
    • The SMRT corepressor is regulated by a MEK-1 kinase pathway: Inhibition of corepressor function is associated with SMRT phosphorylation and nuclear export
    • S.H. Hong, and M.L. Privalsky The SMRT corepressor is regulated by a MEK-1 kinase pathway: inhibition of corepressor function is associated with SMRT phosphorylation and nuclear export Mol. Cell. Biol. 20 2000 6612 6625
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6612-6625
    • Hong, S.H.1    Privalsky, M.L.2
  • 21
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • G.L. Johnson, and R. Lapadat Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases Science 298 2002 1911 1912
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 22
    • 0036093940 scopus 로고    scopus 로고
    • CK2 forms a stable complex with TFIIIB and activates RNA polymerase III transcription in human cells
    • I.M. Johnston, S.J. Allison, J.P. Morton, L. Schramm, P.H. Scott, and R.J. White CK2 forms a stable complex with TFIIIB and activates RNA polymerase III transcription in human cells Mol. Cell. Biol. 22 2002 3757 3768
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3757-3768
    • Johnston, I.M.1    Allison, S.J.2    Morton, J.P.3    Schramm, L.4    Scott, P.H.5    White, R.J.6
  • 23
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29-32
    • R. Koradi, M. Billeter, and K. Wüthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 29-32
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 24
    • 0031911356 scopus 로고    scopus 로고
    • SMADs: Mediators and regulators of TGF-beta signaling
    • M. Kretzschmar, and J. Massagué SMADs: mediators and regulators of TGF-beta signaling Curr. Opin. Genet. Dev. 8 1998 103 111
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 103-111
    • Kretzschmar, M.1    Massagué, J.2
  • 26
    • 0037058999 scopus 로고    scopus 로고
    • Distinct RNA motifs are important for coactivation of steroid hormone receptors by steroid receptor RNA activator (SRA)
    • R.B. Lanz, B. Razani, A.D. Goldberg, and B.W. O'Malley Distinct RNA motifs are important for coactivation of steroid hormone receptors by steroid receptor RNA activator (SRA) Proc. Natl. Acad. Sci. USA 99 2002 16081 16086
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16081-16086
    • Lanz, R.B.1    Razani, B.2    Goldberg, A.D.3    O'Malley, B.W.4
  • 27
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 28
    • 33750207621 scopus 로고    scopus 로고
    • CK2-mediated stimulation of Pol i transcription by stabilization of UBF-SL1 interaction
    • C.Y. Lin, S. Navarro, S. Reddy, and L. Comai CK2-mediated stimulation of Pol I transcription by stabilization of UBF-SL1 interaction Nucleic Acids Res. 34 2006 4752 4766
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4752-4766
    • Lin, C.Y.1    Navarro, S.2    Reddy, S.3    Comai, L.4
  • 30
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • D.W. Litchfield Protein kinase CK2: structure, regulation and role in cellular decisions of life and death Biochem. J. 369 2003 1 15
    • (2003) Biochem. J. , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 31
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • F. Meggio, and L.A. Pinna One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17 2003 349 368
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 32
    • 3142615882 scopus 로고    scopus 로고
    • Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors
    • A. Meinhart, and P. Cramer Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors Nature 430 2004 223 226
    • (2004) Nature , vol.430 , pp. 223-226
    • Meinhart, A.1    Cramer, P.2
  • 33
    • 84883488905 scopus 로고    scopus 로고
    • NMR assignments of SPOC domain of the human transcriptional corepressor SHARP in complex with a C-terminal SMRT peptide
    • S. Mikami, T. Kanaba, Y. Ito, and M. Mishima NMR assignments of SPOC domain of the human transcriptional corepressor SHARP in complex with a C-terminal SMRT peptide Biomol. NMR Assign. 7 2013 267 270
    • (2013) Biomol. NMR Assign. , vol.7 , pp. 267-270
    • Mikami, S.1    Kanaba, T.2    Ito, Y.3    Mishima, M.4
  • 35
    • 0033578427 scopus 로고    scopus 로고
    • The RRM domain of MINT, a novel Msx2 binding protein, recognizes and regulates the rat osteocalcin promoter
    • E.P. Newberry, T. Latifi, and D.A. Towler The RRM domain of MINT, a novel Msx2 binding protein, recognizes and regulates the rat osteocalcin promoter Biochemistry 38 1999 10678 10690
    • (1999) Biochemistry , vol.38 , pp. 10678-10690
    • Newberry, E.P.1    Latifi, T.2    Towler, D.A.3
  • 36
    • 84862195751 scopus 로고    scopus 로고
    • Structural architecture of the human long non-coding RNA, steroid receptor RNA activator
    • I.V. Novikova, S.P. Hennelly, and K.Y. Sanbonmatsu Structural architecture of the human long non-coding RNA, steroid receptor RNA activator Nucleic Acids Res. 40 2012 5034 5051
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5034-5051
    • Novikova, I.V.1    Hennelly, S.P.2    Sanbonmatsu, K.Y.3
  • 38
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • J.V. Olsen, B. Blagoev, F. Gnad, B. Macek, C. Kumar, P. Mortensen, and M. Mann Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 127 2006 635 648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 40
    • 33747029271 scopus 로고    scopus 로고
    • Casein kinase 2 associates with initiation-competent RNA polymerase i and has multiple roles in ribosomal DNA transcription
    • T.B. Panova, K.I. Panov, J. Russell, and J.C. Zomerdijk Casein kinase 2 associates with initiation-competent RNA polymerase I and has multiple roles in ribosomal DNA transcription Mol. Cell. Biol. 26 2006 5957 5968
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5957-5968
    • Panova, T.B.1    Panov, K.I.2    Russell, J.3    Zomerdijk, J.C.4
  • 41
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • L.A. Pinna Protein kinase CK2: a challenge to canons J. Cell Sci. 115 2002 3873 3878
    • (2002) J. Cell Sci. , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 43
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 44
    • 0035339146 scopus 로고    scopus 로고
    • Sharp, an inducible cofactor that integrates nuclear receptor repression and activation
    • Y. Shi, M. Downes, W. Xie, H.Y. Kao, P. Ordentlich, C.C. Tsai, M. Hon, and R.M. Evans Sharp, an inducible cofactor that integrates nuclear receptor repression and activation Genes Dev. 15 2001 1140 1151
    • (2001) Genes Dev. , vol.15 , pp. 1140-1151
    • Shi, Y.1    Downes, M.2    Xie, W.3    Kao, H.Y.4    Ordentlich, P.5    Tsai, C.C.6    Hon, M.7    Evans, R.M.8
  • 46
    • 82655181792 scopus 로고    scopus 로고
    • Nuclear hormone receptor co-repressors: Structure and function
    • P.J. Watson, L. Fairall, and J.W. Schwabe Nuclear hormone receptor co-repressors: structure and function Mol. Cell. Endocrinol. 348 2012 440 449
    • (2012) Mol. Cell. Endocrinol. , vol.348 , pp. 440-449
    • Watson, P.J.1    Fairall, L.2    Schwabe, J.W.3
  • 47
    • 84855984763 scopus 로고    scopus 로고
    • Structure of HDAC3 bound to co-repressor and inositol tetraphosphate
    • P.J. Watson, L. Fairall, G.M. Santos, and J.W. Schwabe Structure of HDAC3 bound to co-repressor and inositol tetraphosphate Nature 481 2012 335 340
    • (2012) Nature , vol.481 , pp. 335-340
    • Watson, P.J.1    Fairall, L.2    Santos, G.M.3    Schwabe, J.W.4
  • 48
    • 84880167453 scopus 로고    scopus 로고
    • Using chemical shift perturbation to characterise ligand binding
    • M.P. Williamson Using chemical shift perturbation to characterise ligand binding Prog. Nucl. Magn. Reson. Spectrosc. 73 2013 1 16
    • (2013) Prog. Nucl. Magn. Reson. Spectrosc. , vol.73 , pp. 1-16
    • Williamson, M.P.1
  • 49
    • 0035080918 scopus 로고    scopus 로고
    • PhosphoSerine/threonine binding domains: You can't pSERious?
    • M.B. Yaffe, and S.J. Smerdon PhosphoSerine/threonine binding domains: you can't pSERious? Structure 9 2001 R33 R38
    • (2001) Structure , vol.9
    • Yaffe, M.B.1    Smerdon, S.J.2
  • 50
    • 84873571381 scopus 로고    scopus 로고
    • Nuclear receptor co-repressors are required for the histone-deacetylase activity of HDAC3 in vivo
    • S.H. You, H.W. Lim, Z. Sun, M. Broache, K.J. Won, and M.A. Lazar Nuclear receptor co-repressors are required for the histone-deacetylase activity of HDAC3 in vivo Nat. Struct. Mol. Biol. 20 2013 182 187
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 182-187
    • You, S.H.1    Lim, H.W.2    Sun, Z.3    Broache, M.4    Won, K.J.5    Lazar, M.A.6
  • 51
    • 0034987964 scopus 로고    scopus 로고
    • The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II)
    • Y. Zhou, W. Gross, S.H. Hong, and M.L. Privalsky The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II) Mol. Cell. Biochem. 220 2001 1 13
    • (2001) Mol. Cell. Biochem. , vol.220 , pp. 1-13
    • Zhou, Y.1    Gross, W.2    Hong, S.H.3    Privalsky, M.L.4


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