메뉴 건너뛰기




Volumn 287, Issue 36, 2012, Pages 30833-30841

Recovery of RNA polymerase III transcription from the glycerol-repressed state: Revisiting the role of protein kinase CK2 in MAF1 phosphoregulation

Author keywords

[No Author keywords available]

Indexed keywords

CARBON SOURCE; DE-REPRESSION; DIVERSE STRESS; FUNCTIONAL MUTANTS; GEL ANALYSIS; HUMAN CELLS; INITIATION FACTORS; MUTANT PROTEINS; NUCLEAR ACCUMULATION; OPTIMAL GROWTH; PHYSICAL INTERACTIONS; PROTEIN KINASE A; PROTEIN KINASE CK2; REGULATED KINASE; RNA POLYMERASE; RNA POLYMERASE III; STRESS CONDITION; TRANSCRIPTIONAL REPRESSION; WILD-TYPE LEVELS;

EID: 84865718223     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.378828     Document Type: Article
Times cited : (13)

References (35)
  • 2
    • 0036923835 scopus 로고    scopus 로고
    • Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription
    • Upadhya, R., Lee, J., and Willis, I. M. (2002) Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription. Mol. Cell 10, 1489-1494
    • (2002) Mol. Cell , vol.10 , pp. 1489-1494
    • Upadhya, R.1    Lee, J.2    Willis, I.M.3
  • 3
    • 33846659385 scopus 로고    scopus 로고
    • Integration of nutritional and stress signaling pathways by Maf1
    • Willis, I. M., and Moir, R. D. (2007) Integration of nutritional and stress signaling pathways by Maf1. Trends Biochem. Sci. 32, 51-53
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 51-53
    • Willis, I.M.1    Moir, R.D.2
  • 4
    • 77957658806 scopus 로고    scopus 로고
    • Maf1 regulation: A model of signal transduction inside the nucleus
    • Wei, Y., and Zheng, X. S. (2010) Maf1 regulation: a model of signal transduction inside the nucleus. Nucleus 1, 162-165
    • (2010) Nucleus , vol.1 , pp. 162-165
    • Wei, Y.1    Zheng, X.S.2
  • 5
    • 4143077932 scopus 로고    scopus 로고
    • Signaling repression of transcription by RNA polymerase III in yeast
    • Willis, I. M., Desai, N. A., and Upadhya, R. (2004) Signaling repression of transcription by RNA polymerase III in yeast Prog. Nucleic Acids Res. Mol. Biol. 77, 323-353
    • (2004) Prog. Nucleic Acids Res. Mol. Biol. , vol.77 , pp. 323-353
    • Willis, I.M.1    Desai, N.A.2    Upadhya, R.3
  • 6
    • 33749257174 scopus 로고    scopus 로고
    • Protein kinase A regulates RNA polymerase III transcription through the nuclear localization of Maf1
    • Moir, R. D., Lee, J., Haeusler, R. A., Desai, N., Engelke, D. R., and Willis, I. M. (2006) Protein kinase A regulates RNA polymerase III transcription through the nuclear localization of Maf1. Proc. Natl. Acad. Sci. U.S.A. 103, 15044-15049
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15044-15049
    • Moir, R.D.1    Lee, J.2    Haeusler, R.A.3    Desai, N.4    Engelke, D.R.5    Willis, I.M.6
  • 7
    • 69249240179 scopus 로고    scopus 로고
    • Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis
    • Huber, A., Bodenmiller, B., Uotila, A., Stahl, M., Wanka, S., Gerrits, B., Aebersold, R., and Loewith, R. (2009) Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis Genes Dev. 23, 1929-1943
    • (2009) Genes Dev. , vol.23 , pp. 1929-1943
    • Huber, A.1    Bodenmiller, B.2    Uotila, A.3    Stahl, M.4    Wanka, S.5    Gerrits, B.6    Aebersold, R.7    Loewith, R.8
  • 8
    • 84862789978 scopus 로고    scopus 로고
    • TOR signaling regulates ribosome and tRNA synthesis via LAMMER/Clk and GSK-3 family kinases
    • Lee, J., Moir, R. D., McIntosh, K. B., and Willis, I. M. (2012) TOR signaling regulates ribosome and tRNA synthesis via LAMMER/Clk and GSK-3 family kinases. Mol. Cell 45, 836-843
    • (2012) Mol. Cell , vol.45 , pp. 836-843
    • Lee, J.1    Moir, R.D.2    McIntosh, K.B.3    Willis, I.M.4
  • 9
    • 14844318502 scopus 로고    scopus 로고
    • Two steps in Maf1-dependent repression of transcription by RNA polymerase III
    • Desai, N., Lee, J., Upadhya, R., Chu, Y., Moir, R. D., and Willis, I. M. (2005) Two steps in Maf1-dependent repression of transcription by RNA polymerase III. J. Biol. Chem. 280, 6455-6462
    • (2005) J. Biol. Chem. , vol.280 , pp. 6455-6462
    • Desai, N.1    Lee, J.2    Upadhya, R.3    Chu, Y.4    Moir, R.D.5    Willis, I.M.6
  • 10
    • 54949143524 scopus 로고    scopus 로고
    • Maf1, a New Player in the Regulation of Human RNA Polymerase III Transcription
    • Reina, J. H., Azzouz, T. N., and Hernandez, N. (2006) Maf1, a New Player in the Regulation of Human RNA Polymerase III Transcription. PLoS. ONE. 1, e134
    • (2006) PLoS. ONE , vol.1
    • Reina, J.H.1    Azzouz, T.N.2    Hernandez, N.3
  • 11
    • 61349155582 scopus 로고    scopus 로고
    • Facilitated recycling protects human RNA polymerase III from repression by Maf1 in vitro
    • Cabart, P., Lee, J., and Willis, I. M. (2008) Facilitated recycling protects human RNA polymerase III from repression by Maf1 in vitro. J. Biol. Chem. 283, 36108-36117
    • (2008) J. Biol. Chem. , vol.283 , pp. 36108-36117
    • Cabart, P.1    Lee, J.2    Willis, I.M.3
  • 13
    • 67649827419 scopus 로고    scopus 로고
    • Regulation of RNA polymerase III transcription involves SCH9-dependent and SCH9-independent branches of the target of rapamycin (TOR) pathway
    • Lee, J., Moir, R. D., and Willis, I. M. (2009) Regulation of RNA polymerase III transcription involves SCH9-dependent and SCH9-independent branches of the target of rapamycin (TOR) pathway. J. Biol. Chem. 284, 12604-12608
    • (2009) J. Biol. Chem. , vol.284 , pp. 12604-12608
    • Lee, J.1    Moir, R.D.2    Willis, I.M.3
  • 14
    • 74849135206 scopus 로고    scopus 로고
    • Sch9 partially mediates TORC1 signaling to control ribosomal RNA synthesis
    • Wei, Y., and Zheng, X. F. (2009) Sch9 partially mediates TORC1 signaling to control ribosomal RNA synthesis Cell Cycle 8, 4085-4090
    • (2009) Cell Cycle , vol.8 , pp. 4085-4090
    • Wei, Y.1    Zheng, X.F.2
  • 16
    • 77952036652 scopus 로고    scopus 로고
    • Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control ofRNApolymerase III-dependent transcription in cancer cells
    • Shor, B., Wu, J., Shakey, Q., Toral-Barza, L., Shi, C., Follettie, M., and Yu, K. (2010) Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control ofRNApolymerase III-dependent transcription in cancer cells. J. Biol. Chem. 285, 15380-15392
    • (2010) J. Biol. Chem. , vol.285 , pp. 15380-15392
    • Shor, B.1    Wu, J.2    Shakey, Q.3    Toral-Barza, L.4    Shi, C.5    Follettie, M.6    Yu, K.7
  • 17
    • 77955287244 scopus 로고    scopus 로고
    • mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1
    • Kantidakis, T., Ramsbottom, B. A., Birch, J. L., Dowding, S. N., and White, R. J. (2010) mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1. Proc. Natl. Acad. Sci. U.S.A. 107, 11823-11828
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11823-11828
    • Kantidakis, T.1    Ramsbottom, B.A.2    Birch, J.L.3    Dowding, S.N.4    White, R.J.5
  • 18
    • 70349186117 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: From birth to death: The role of protein kinase CK2 in the regulation of cell proliferation and survival
    • St Denis, N. A., and Litchfield, D. W. (2009) Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival. Cell Mol Life Sci. 66, 1817-1829
    • (2009) Cell Mol Life Sci. , vol.66 , pp. 1817-1829
    • St Denis, N.A.1    Litchfield, D.W.2
  • 19
    • 0035823010 scopus 로고    scopus 로고
    • TATA binding protein-associated CK2 transduces DNA damage signals to the RNA polymerase III transcriptional machinery
    • Ghavidel, A., and Schultz, M. C. (2001) TATA binding protein-associated CK2 transduces DNA damage signals to the RNA polymerase III transcriptional machinery. Cell 106, 575-584
    • (2001) Cell , vol.106 , pp. 575-584
    • Ghavidel, A.1    Schultz, M.C.2
  • 20
    • 0036093940 scopus 로고    scopus 로고
    • CK2 forms a stable complex with TFIIIB and activates RNA polymerase III transcription in human cells
    • Johnston, I. M., Allison, S. J., Morton, J. P., Schramm, L., Scott, P. H., and White, R. J. (2002) CK2 forms a stable complex with TFIIIB and activates RNA polymerase III transcription in human cells. Mol. Cell. Biol. 22, 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
  • 21
    • 0141750428 scopus 로고    scopus 로고
    • Minimal RNA polymerase III transcription system from human cells reveals positive and negative regulatory roles for CK2
    • Hu, P., Wu, S., and Hernandez, N. A. (2003) Minimal RNA polymerase III transcription system from human cells reveals positive and negative regulatory roles for CK2. Mol. Cell 12, 699-709
    • (2003) Mol. Cell , vol.12 , pp. 699-709
    • Hu, P.1    Wu, S.2    Hernandez, N.A.3
  • 22
    • 79952262287 scopus 로고    scopus 로고
    • Genome stability control by checkpoint regulation of tRNA gene transcription
    • Clelland, B. W., and Schultz, M. C. (2010) Genome stability control by checkpoint regulation of tRNA gene transcription. Transcription 1, 115-125
    • (2010) Transcription , vol.1 , pp. 115-125
    • Clelland, B.W.1    Schultz, M.C.2
  • 23
    • 70349336104 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: A dynamic affair
    • Filhol, O., and Cochet, C. (2009) Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair. Cell Mol. Life Sci. 66, 1830-1839
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1830-1839
    • Filhol, O.1    Cochet, C.2
  • 24
    • 4944253296 scopus 로고    scopus 로고
    • CK2 phosphorylation of Bdp1 executes cell cycle-specific RNA polymerase III transcription repression
    • Hu, P., Samudre, K., Wu, S., Sun, Y., and Hernandez, N. (2004) CK2 phosphorylation of Bdp1 executes cell cycle-specific RNA polymerase III transcription repression. Mol. Cell 16, 81-92
    • (2004) Mol. Cell , vol.16 , pp. 81-92
    • Hu, P.1    Samudre, K.2    Wu, S.3    Sun, Y.4    Hernandez, N.5
  • 25
    • 79953192187 scopus 로고    scopus 로고
    • Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation
    • Graczyk, D., Debski, J., Muszyńska, G., Bretner, M., Lefebvre, O., and Boguta, M. (2011) Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation. Proc. Natl. Acad. Sci. U.S.A. 108, 4926-4931
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 4926-4931
    • Graczyk, D.1    Debski, J.2    Muszyńska, G.3    Bretner, M.4    Lefebvre, O.5    Boguta, M.6
  • 26
    • 79961052749 scopus 로고    scopus 로고
    • Does casein kinase II phosphorylation of Maf1 trigger RNA polymerase III activation?
    • Willis, I. M., Moir, R. D., and Lee, J. (2011) Does casein kinase II phosphorylation of Maf1 trigger RNA polymerase III activation? Proc. Natl. Acad. Sci. U.S.A. 108, E300
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Willis, I.M.1    Moir, R.D.2    Lee, J.3
  • 27
    • 84865773882 scopus 로고    scopus 로고
    • Phosphopeptide characterization by mass spectrometry using reversedphase supports for solid-phase beta-elimination/michael addition
    • Nika, H., Lee, J., Willis, I. M., Angeletti, R. H., and Hawke, D. H. (2012) Phosphopeptide characterization by mass spectrometry using reversedphase supports for solid-phase beta-elimination/michael addition J. Biomol. Tech. 23, 51-68
    • (2012) J. Biomol. Tech. , vol.23 , pp. 51-68
    • Nika, H.1    Lee, J.2    Willis, I.M.3    Angeletti, R.H.4    Hawke, D.H.5
  • 29
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): Management, structural, and evolutionary investigation, and prediction of phosphosites
    • Gnad, F., Ren, S., Cox, J., Olsen, J., Macek, B., Oroshi, M., and Mann, M. (2007) PHOSIDA (phosphorylation site database): management, structural, and evolutionary investigation, and prediction of phosphosites. Genome Biol. 8, R250
    • (2007) Genome Biol. , vol.8
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.4    Macek, B.5    Oroshi, M.6    Mann, M.7
  • 31
    • 33744515555 scopus 로고    scopus 로고
    • Dephosphorylation and genome-wide association of Maf1 with Pol III-transcribed genes during repression
    • Roberts, D. N., Wilson, B., Huff, J. T., Stewart, A. J., and Cairns, B. R. (2006) Dephosphorylation and genome-wide association of Maf1 with Pol III-transcribed genes during repression. Mol. Cell 22, 633-644
    • (2006) Mol. Cell , vol.22 , pp. 633-644
    • Roberts, D.N.1    Wilson, B.2    Huff, J.T.3    Stewart, A.J.4    Cairns, B.R.5
  • 32
    • 33744512096 scopus 로고    scopus 로고
    • General repression of RNA polymerase III transcription is triggered by protein phosphatase Type 2A-mediated dephosphorylation of Maf1
    • Oficjalska-Pham, D., Harismendy, O., Smagowicz, W. J., Gonzalez, de Peredo, A., Boguta, M., Sentenac, A., and Lefebvre, O. (2006) General repression of RNA polymerase III transcription is triggered by protein phosphatase Type 2A-mediated dephosphorylation of Maf1. Mol. Cell 22, 623-632
    • (2006) Mol. Cell , vol.22 , pp. 623-632
    • Oficjalska-Pham, D.1    Harismendy, O.2    Smagowicz, W.J.3    Gonzalez4    De Peredo, A.5    Boguta, M.6    Sentenac, A.7    Lefebvre, O.8
  • 33
    • 77958031723 scopus 로고    scopus 로고
    • The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates
    • Soulard, A., Cremonesi, A., Moes, S., Schütz, F., Jeno, P., and Hall, M. N. (2010) The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Mol. Biol. Cell 21, 3475-3486
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3475-3486
    • Soulard, A.1    Cremonesi, A.2    Moes, S.3    Schütz, F.4    Jeno, P.5    Hall, M.N.6
  • 34
    • 34948828483 scopus 로고    scopus 로고
    • Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae
    • Yorimitsu, T., Zaman, S., Broach, J. R., and Klionsky, D. J. (2007) Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae. Mol. Biol. Cell 18, 4180-4189
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4180-4189
    • Yorimitsu, T.1    Zaman, S.2    Broach, J.R.3    Klionsky, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.