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•] identifies Dot6/Tod6 as RRPE element binding transcription factors and Ribi gene regulators in yeast.
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(2009)
Genome Res
, vol.19
, pp. 556-566
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Zhu, C.1
Byers, K.J.2
McCord, R.P.3
Shi, Z.4
Berger, M.F.5
Newburger, D.E.6
Saulrieta, K.7
Smith, Z.8
Shah, M.V.9
Radhakrishnan, M.10
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38
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Microarray profiling of phage-display selections for rapid mapping of transcription factor-DNA interactions
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•] identifies Dot6/Tod6 as RRPE element binding proteins and Ribi gene regulators in yeast.
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•] identifies Dot6/Tod6 as RRPE element binding proteins and Ribi gene regulators in yeast.
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(2009)
PLoS Genet
, vol.5
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Freckleton, G.1
Lippman, S.I.2
Broach, J.R.3
Tavazoie, S.4
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39
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Myc's broad reach
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Excellent review on Myc signalling.
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Eilers M., and Eisenman R.N. Myc's broad reach. Genes Dev 22 (2008) 2755-2766. Excellent review on Myc signalling.
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, pp. 2755-2766
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Eilers, M.1
Eisenman, R.N.2
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40
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33646843753
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Activation by c-Myc of transcription by RNA polymerases I, II and III
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Gomez-Roman N., Felton-Edkins Z.A., Kenneth N.S., Goodfellow S.J., Athineos D., Zhang J., Ramsbottom B.A., Innes F., Kantidakis T., Kerr E.R., et al. Activation by c-Myc of transcription by RNA polymerases I, II and III. Biochem Soc Symp 73 (2006) 141-154
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Biochem Soc Symp
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, pp. 141-154
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Gomez-Roman, N.1
Felton-Edkins, Z.A.2
Kenneth, N.S.3
Goodfellow, S.J.4
Athineos, D.5
Zhang, J.6
Ramsbottom, B.A.7
Innes, F.8
Kantidakis, T.9
Kerr, E.R.10
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41
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0034952725
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Maf1p, a negative effector of RNA polymerase III in Saccharomyces cerevisiae
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Pluta K., Lefebvre O., Martin N.C., Smagowicz W.J., Stanford D.R., Ellis S.R., Hopper A.K., Sentenac A., and Boguta M. Maf1p, a negative effector of RNA polymerase III in Saccharomyces cerevisiae. Mol Cell Biol 21 (2001) 5031-5040
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(2001)
Mol Cell Biol
, vol.21
, pp. 5031-5040
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Pluta, K.1
Lefebvre, O.2
Martin, N.C.3
Smagowicz, W.J.4
Stanford, D.R.5
Ellis, S.R.6
Hopper, A.K.7
Sentenac, A.8
Boguta, M.9
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42
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Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription
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Upadhya R., Lee J., and Willis I.M. Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription. Mol Cell 10 (2002) 1489-1494
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(2002)
Mol Cell
, vol.10
, pp. 1489-1494
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Upadhya, R.1
Lee, J.2
Willis, I.M.3
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43
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Regulation of RNA polymerase III transcription by Maf1 protein
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Ciesla M., and Boguta M. Regulation of RNA polymerase III transcription by Maf1 protein. Acta Biochim Pol 55 (2008) 215-225
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(2008)
Acta Biochim Pol
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, pp. 215-225
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Ciesla, M.1
Boguta, M.2
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44
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33846659385
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Integration of nutritional and stress signaling pathways by Maf1
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Willis I.M., and Moir R.D. Integration of nutritional and stress signaling pathways by Maf1. Trends Biochem Sci 32 (2007) 51-53
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(2007)
Trends Biochem Sci
, vol.32
, pp. 51-53
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Willis, I.M.1
Moir, R.D.2
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45
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34247553679
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Mammalian Maf1 is a negative regulator of transcription by all three nuclear RNA polymerases
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This paper shows that Maf1 negatively regulates all three nuclear RNAPs. In part, the effect of Maf1 on RNAP I and RNAP III operates through repression of the gene encoding the TATA-binding protein, TBP. The repressive effect of Maf1 is associated with direct promoter binding, whose magnitude is reciprocal to that of Elk-1 at the TBP promoter, and with TFIIIB and RNAP III at Pol III promoters.
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Johnson S.S., Zhang C., Fromm J., Willis I.M., and Johnson D.L. Mammalian Maf1 is a negative regulator of transcription by all three nuclear RNA polymerases. Mol Cell 26 (2007) 367-379. This paper shows that Maf1 negatively regulates all three nuclear RNAPs. In part, the effect of Maf1 on RNAP I and RNAP III operates through repression of the gene encoding the TATA-binding protein, TBP. The repressive effect of Maf1 is associated with direct promoter binding, whose magnitude is reciprocal to that of Elk-1 at the TBP promoter, and with TFIIIB and RNAP III at Pol III promoters.
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(2007)
Mol Cell
, vol.26
, pp. 367-379
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Johnson, S.S.1
Zhang, C.2
Fromm, J.3
Willis, I.M.4
Johnson, D.L.5
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46
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67649827419
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Regulation of RNA polymerase III transcription involves SCH9-dependent and -independent branches of the TOR pathway
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This paper shows that the Sch9 kinase is a positive regulator of RNAP III transcription that acts by phosphorylating, and thereby inactivating, Maf1. Evidence is presented for additional, Sch9-independent pathway(s) of TOR signaling that regulates RNAP III activity.
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Lee J., Moir R.D., and Willis I.M. Regulation of RNA polymerase III transcription involves SCH9-dependent and -independent branches of the TOR pathway. J Biol Chem 284 (2009) 12604-12608. This paper shows that the Sch9 kinase is a positive regulator of RNAP III transcription that acts by phosphorylating, and thereby inactivating, Maf1. Evidence is presented for additional, Sch9-independent pathway(s) of TOR signaling that regulates RNAP III activity.
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(2009)
J Biol Chem
, vol.284
, pp. 12604-12608
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Lee, J.1
Moir, R.D.2
Willis, I.M.3
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47
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69249240179
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Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis
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In this paper the author utilize a state-of-art mass spectrometry screen to characterize the rapamycin-sensitive phophoproteome in yeast. The screen identifies Sch9 as a major regulator of protein synthesis and the authors further show that Sch9 directly phosphorylates and regulates Maf1.
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Huber A., Bodenmiller B., Uotila A., Stahl M., Wanka S., Gerrits B., Aebersold R., and Loewith R. Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis. Genes Dev 23 (2009) 1929-1943. In this paper the author utilize a state-of-art mass spectrometry screen to characterize the rapamycin-sensitive phophoproteome in yeast. The screen identifies Sch9 as a major regulator of protein synthesis and the authors further show that Sch9 directly phosphorylates and regulates Maf1.
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(2009)
Genes Dev
, vol.23
, pp. 1929-1943
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Huber, A.1
Bodenmiller, B.2
Uotila, A.3
Stahl, M.4
Wanka, S.5
Gerrits, B.6
Aebersold, R.7
Loewith, R.8
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48
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33746631755
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The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components
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The authors generate a yeast strain in which RNAP I is deregulated through gene fusion of the Rpa43 subunit to RNAP III to the recruited activator Rrn3 (TIF-1A in mammals). Remarkably, the CARA (Constitutive Association of Rpa43 and A43) strain also displays defective downregulation of RP genes and 5S transcription, for example in response to rapamycin inhibition of TORC1. These data suggest that some aspect of rRNA transcription and/or processing exerts a regulatory effect on RNAP II transcription of RP genes and RNAP III transcription of 5S rRNA.
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Laferte A., Favry E., Sentenac A., Riva M., Carles C., and Chedin S. The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components. Genes Dev 20 (2006) 2030-2040. The authors generate a yeast strain in which RNAP I is deregulated through gene fusion of the Rpa43 subunit to RNAP III to the recruited activator Rrn3 (TIF-1A in mammals). Remarkably, the CARA (Constitutive Association of Rpa43 and A43) strain also displays defective downregulation of RP genes and 5S transcription, for example in response to rapamycin inhibition of TORC1. These data suggest that some aspect of rRNA transcription and/or processing exerts a regulatory effect on RNAP II transcription of RP genes and RNAP III transcription of 5S rRNA.
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(2006)
Genes Dev
, vol.20
, pp. 2030-2040
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Laferte, A.1
Favry, E.2
Sentenac, A.3
Riva, M.4
Carles, C.5
Chedin, S.6
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49
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33846614928
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Is ribosome synthesis controlled by pol I transcription?
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Chedin S., Laferte A., Hoang T., Lafontaine D.L., Riva M., and Carles C. Is ribosome synthesis controlled by pol I transcription?. Cell Cycle 6 (2007) 11-15
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(2007)
Cell Cycle
, vol.6
, pp. 11-15
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Chedin, S.1
Laferte, A.2
Hoang, T.3
Lafontaine, D.L.4
Riva, M.5
Carles, C.6
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50
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34347336512
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Potential interface between ribosomal protein production and pre-rRNA processing
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Ifh1, recruited by Fhl1 to activate RP genes, is shown here to be present in a complex (called 'CURI') with the four casein kinase 2 (CK2) subunits and two proteins involved in rRNA processing, Utp22 and Rrp7. Depletion of Utp22 or Rrp7, but not other rRNA processing factors, leads to increased RP mRNA levels. The authors propose that the CURI complex provides a regulatory link between RNAP I and the RNAP II-mediated transcription of RP genes, and suggest, among other possibilities, that CURI might act to sequester Ifh1 from RP gene promoters.
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Rudra D., Mallick J., Zhao Y., and Warner J.R. Potential interface between ribosomal protein production and pre-rRNA processing. Mol Cell Biol 27 (2007) 4815-4824. Ifh1, recruited by Fhl1 to activate RP genes, is shown here to be present in a complex (called 'CURI') with the four casein kinase 2 (CK2) subunits and two proteins involved in rRNA processing, Utp22 and Rrp7. Depletion of Utp22 or Rrp7, but not other rRNA processing factors, leads to increased RP mRNA levels. The authors propose that the CURI complex provides a regulatory link between RNAP I and the RNAP II-mediated transcription of RP genes, and suggest, among other possibilities, that CURI might act to sequester Ifh1 from RP gene promoters.
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(2007)
Mol Cell Biol
, vol.27
, pp. 4815-4824
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Rudra, D.1
Mallick, J.2
Zhao, Y.3
Warner, J.R.4
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51
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64049107857
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Absence of nucleolar disruption after impairment of 40S ribosome biogenesis reveals an rpL11-translation-dependent mechanism of p53 induction
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This paper shows that depletion of rps6, either by tissue-specific knockout in whole animals or siRNA in cultured cells, induces rpL11 overexpression, inhibition of MDM2 and p53-mediated cell-cycle arrest, all in the absence of nucleolar disruption. Instead, they find that disruption of 40S ribosome biogenesis leads to increased translation of 5′-TOP mRNAs, including that of rpL11. The authors suggest that rpL11 might thus be a useful therapeutic target in human disorders involving 40S components, thereby leaving p53 free for induction by other potentially beneficial stress pathways.
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Fumagalli S., Di Cara A., Neb-Gulati A., Natt F., Schwemberger S., Hall J., Babcock G.F., Bernardi R., Pandolfi P.P., and Thomas G. Absence of nucleolar disruption after impairment of 40S ribosome biogenesis reveals an rpL11-translation-dependent mechanism of p53 induction. Nat Cell Biol 11 (2009) 501-508. This paper shows that depletion of rps6, either by tissue-specific knockout in whole animals or siRNA in cultured cells, induces rpL11 overexpression, inhibition of MDM2 and p53-mediated cell-cycle arrest, all in the absence of nucleolar disruption. Instead, they find that disruption of 40S ribosome biogenesis leads to increased translation of 5′-TOP mRNAs, including that of rpL11. The authors suggest that rpL11 might thus be a useful therapeutic target in human disorders involving 40S components, thereby leaving p53 free for induction by other potentially beneficial stress pathways.
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(2009)
Nat Cell Biol
, vol.11
, pp. 501-508
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Fumagalli, S.1
Di Cara, A.2
Neb-Gulati, A.3
Natt, F.4
Schwemberger, S.5
Hall, J.6
Babcock, G.F.7
Bernardi, R.8
Pandolfi, P.P.9
Thomas, G.10
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52
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34547151021
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Inhibition of c-Myc activity by ribosomal protein L11
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Previous studies showed that the gene encoding rpL11 is activated by c-Myc. Here the authors show that overexpression of rpL11 downregulates c-Myc-driven transcription of a reporter gene as well as endogenous c-Myc-targeted genes. An N-terminal domain of rpL11 binds directly to c-Myc in vitro, and this binding requires a specific motif (MB-II) in the c-Myc transcriptional activation domain. RpL11 co-occupies c-Myc target genes in vivo, and evidence is presented indicating that the rpL11-c-Myc interaction blocks recruitment of the TRRAP coactivator complex, thus reducing histone H4 acetylation at target promoters. Taken together, these data provide evidence that rpL11 is a feedback inhibitor of c-Myc.
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Dai M.S., Arnold H., Sun X.X., Sears R., and Lu H. Inhibition of c-Myc activity by ribosomal protein L11. EMBO J 26 (2007) 3332-3345. Previous studies showed that the gene encoding rpL11 is activated by c-Myc. Here the authors show that overexpression of rpL11 downregulates c-Myc-driven transcription of a reporter gene as well as endogenous c-Myc-targeted genes. An N-terminal domain of rpL11 binds directly to c-Myc in vitro, and this binding requires a specific motif (MB-II) in the c-Myc transcriptional activation domain. RpL11 co-occupies c-Myc target genes in vivo, and evidence is presented indicating that the rpL11-c-Myc interaction blocks recruitment of the TRRAP coactivator complex, thus reducing histone H4 acetylation at target promoters. Taken together, these data provide evidence that rpL11 is a feedback inhibitor of c-Myc.
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(2007)
EMBO J
, vol.26
, pp. 3332-3345
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Dai, M.S.1
Arnold, H.2
Sun, X.X.3
Sears, R.4
Lu, H.5
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53
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48549094467
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c-Myc and eIF4F are components of a feedforward loop that links transcription and translation
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This report shows that c-Myc is a direct transcriptional activator of genes encoding the heterotrimeric eIF4F complex (eIF4E, eIF4AI, and eIF4GI), which binds to the 5′ CAP structure of mRNAs and plays a key role in translation initiation. The eIF4F complex is in turn shown to specifically stimulate c-Myc mRNA translation. These data support the idea that c-Myc and eIF4F function in a feedforward loop linking transcription and translation that might contribute to the proliferative effects of c-Myc, including those promoting ribosome biogenesis.
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Lin C.J., Cencic R., Mills J.R., Robert F., and Pelletier J. c-Myc and eIF4F are components of a feedforward loop that links transcription and translation. Cancer Res 68 (2008) 5326-5334. This report shows that c-Myc is a direct transcriptional activator of genes encoding the heterotrimeric eIF4F complex (eIF4E, eIF4AI, and eIF4GI), which binds to the 5′ CAP structure of mRNAs and plays a key role in translation initiation. The eIF4F complex is in turn shown to specifically stimulate c-Myc mRNA translation. These data support the idea that c-Myc and eIF4F function in a feedforward loop linking transcription and translation that might contribute to the proliferative effects of c-Myc, including those promoting ribosome biogenesis.
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(2008)
Cancer Res
, vol.68
, pp. 5326-5334
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Lin, C.J.1
Cencic, R.2
Mills, J.R.3
Robert, F.4
Pelletier, J.5
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54
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43449090367
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MicroRNA-10a binds the 5′ UTR of ribosomal protein mRNAs and enhances their translation
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This report shows that microRNA-10a binds to a conserved sequence immediately downstream of the 5′-TOP in RP gene mRNAs. Surprisingly, this interaction stimulates translation of the RP mRNA targets. miR-10a can counteract translational repression of RP mRNAs during amino acid starvation and is required for their translational induction following anisomycin treatment or RAS overexpression. This study thus raises the possibility that microRNA-10a provides a regulatory input to control RP expression at the translational levels, and provides evidence that its action could promote oncogenic transformation.
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Orom U.A., Nielsen F.C., and Lund A.H. MicroRNA-10a binds the 5′ UTR of ribosomal protein mRNAs and enhances their translation. Mol Cell 30 (2008) 460-471. This report shows that microRNA-10a binds to a conserved sequence immediately downstream of the 5′-TOP in RP gene mRNAs. Surprisingly, this interaction stimulates translation of the RP mRNA targets. miR-10a can counteract translational repression of RP mRNAs during amino acid starvation and is required for their translational induction following anisomycin treatment or RAS overexpression. This study thus raises the possibility that microRNA-10a provides a regulatory input to control RP expression at the translational levels, and provides evidence that its action could promote oncogenic transformation.
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(2008)
Mol Cell
, vol.30
, pp. 460-471
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Orom, U.A.1
Nielsen, F.C.2
Lund, A.H.3
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55
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10344222155
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How cells coordinate growth and division
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Jorgensen P., and Tyers M. How cells coordinate growth and division. Curr Biol 14 (2004) R1014-1027
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(2004)
Curr Biol
, vol.14
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Jorgensen, P.1
Tyers, M.2
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56
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33947183025
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Ribosome biogenesis is sensed at the Start cell cycle checkpoint
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Inducible depletion of an rRNA processing factor (Pwp2/Utp1) is used to examine the effect of ribosome biogenesis on cell-cycle progression. The authors show that this leads to a delay in entry into the cell cycle (START), in particular by an expansion of the early phase of G1 when the Rb-like transcriptional regulator Whi5 is still nuclear. This delay occurs before any effect on ribosome number or translation can be detected. When Whi5 is deleted cells cannot delay G1 in response to a ribosome biogenesis defect. Taken together, these data suggest that cells sense some aspect of ribosome biogenesis in order to control cell-cycle entry and cell size.
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Bernstein K.A., Bleichert F., Bean J.M., Cross F.R., and Baserga S.J. Ribosome biogenesis is sensed at the Start cell cycle checkpoint. Mol Biol Cell 18 (2007) 953-964. Inducible depletion of an rRNA processing factor (Pwp2/Utp1) is used to examine the effect of ribosome biogenesis on cell-cycle progression. The authors show that this leads to a delay in entry into the cell cycle (START), in particular by an expansion of the early phase of G1 when the Rb-like transcriptional regulator Whi5 is still nuclear. This delay occurs before any effect on ribosome number or translation can be detected. When Whi5 is deleted cells cannot delay G1 in response to a ribosome biogenesis defect. Taken together, these data suggest that cells sense some aspect of ribosome biogenesis in order to control cell-cycle entry and cell size.
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(2007)
Mol Biol Cell
, vol.18
, pp. 953-964
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Bernstein, K.A.1
Bleichert, F.2
Bean, J.M.3
Cross, F.R.4
Baserga, S.J.5
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57
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65549142204
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A role for ubiquitin in selective autophagy
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Kirkin V., McEwan D.G., Novak I., and Dikic I. A role for ubiquitin in selective autophagy. Mol Cell 34 (2009) 259-269
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(2009)
Mol Cell
, vol.34
, pp. 259-269
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Kirkin, V.1
McEwan, D.G.2
Novak, I.3
Dikic, I.4
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58
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43049138051
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Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
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Using a visual screen of a library of single-gene deletions in yeast, the authors show that selective autophagic degradation of ribosomes upon nutrient stress requires the ubiquitin protease Ubp3/Bre5. The accumulation of ubiquitinylated RPs and/or ribosome-associated proteins in ubp3-cells suggests that ubiquitinylation may directly regulate 40S autophagy. The fact that ubp3-mutants are both nutrient starvation and rapamycin sensitive suggests that 'ribophagy' may be important for survival under stress conditions.
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Kraft C., Deplazes A., Sohrmann M., and Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol 10 (2008) 602-610. Using a visual screen of a library of single-gene deletions in yeast, the authors show that selective autophagic degradation of ribosomes upon nutrient stress requires the ubiquitin protease Ubp3/Bre5. The accumulation of ubiquitinylated RPs and/or ribosome-associated proteins in ubp3-cells suggests that ubiquitinylation may directly regulate 40S autophagy. The fact that ubp3-mutants are both nutrient starvation and rapamycin sensitive suggests that 'ribophagy' may be important for survival under stress conditions.
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(2008)
Nat Cell Biol
, vol.10
, pp. 602-610
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Kraft, C.1
Deplazes, A.2
Sohrmann, M.3
Peter, M.4
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59
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33751316103
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A late-acting quality control process for mature eukaryotic rRNAs
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LaRiviere F.J., Cole S.E., Ferullo D.J., and Moore M.J. A late-acting quality control process for mature eukaryotic rRNAs. Mol Cell 24 (2006) 619-626
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(2006)
Mol Cell
, vol.24
, pp. 619-626
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LaRiviere, F.J.1
Cole, S.E.2
Ferullo, D.J.3
Moore, M.J.4
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60
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65249168677
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A role for ubiquitin in the clearance of nonfunctional rRNAs
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This paper shows that nonfunctional rRNA decay in yeast, a pathway for selective degradation of defective rRNA molecules, requires the Rtt101 and Mms1 ubiquitin E3 ligase components, both previously identified as factors involved in DNA repair. The authors suggest that this constitutes a conserved cellular response to genotoxic stress that is harmful to both DNA and rRNA.
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Fujii K., Kitabatake M., Sakata T., Miyata A., and Ohno M. A role for ubiquitin in the clearance of nonfunctional rRNAs. Genes Dev 23 (2009) 963-974. This paper shows that nonfunctional rRNA decay in yeast, a pathway for selective degradation of defective rRNA molecules, requires the Rtt101 and Mms1 ubiquitin E3 ligase components, both previously identified as factors involved in DNA repair. The authors suggest that this constitutes a conserved cellular response to genotoxic stress that is harmful to both DNA and rRNA.
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(2009)
Genes Dev
, vol.23
, pp. 963-974
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Fujii, K.1
Kitabatake, M.2
Sakata, T.3
Miyata, A.4
Ohno, M.5
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61
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34247391127
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Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
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The paper reports that in HeLa cells ribosomal proteins are expressed at much higher levels than required for the typical rate of ribosome-subunit production and this is balanced by degradation of unassembled ribosomal proteins in the nucleus.
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Lam Y.W., Lamond A.I., Mann M., and Andersen J.S. Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr Biol 17 (2007) 749-760. The paper reports that in HeLa cells ribosomal proteins are expressed at much higher levels than required for the typical rate of ribosome-subunit production and this is balanced by degradation of unassembled ribosomal proteins in the nucleus.
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(2007)
Curr Biol
, vol.17
, pp. 749-760
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Lam, Y.W.1
Lamond, A.I.2
Mann, M.3
Andersen, J.S.4
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62
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34249748415
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Building ribosomes: even more expensive than expected?
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Granneman S., and Tollervey D. Building ribosomes: even more expensive than expected?. Curr Biol 17 (2007) R415-417
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(2007)
Curr Biol
, vol.17
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Granneman, S.1
Tollervey, D.2
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63
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42049099544
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Ribosomal dysfunction and inherited marrow failure
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Ganapathi K.A., and Shimamura A. Ribosomal dysfunction and inherited marrow failure. Br J Haematol 141 (2008) 376-387
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(2008)
Br J Haematol
, vol.141
, pp. 376-387
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Ganapathi, K.A.1
Shimamura, A.2
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64
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0037363075
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Does the ribosome translate cancer?
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Ruggero D., and Pandolfi P.P. Does the ribosome translate cancer?. Nat Rev Cancer 3 (2003) 179-192
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(2003)
Nat Rev Cancer
, vol.3
, pp. 179-192
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Ruggero, D.1
Pandolfi, P.P.2
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65
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19344366193
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Many ribosomal protein genes are cancer genes in zebrafish
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Amsterdam A., Sadler K.C., Lai K., Farrington S., Bronson R.T., Lees J.A., and Hopkins N. Many ribosomal protein genes are cancer genes in zebrafish. PLoS Biol 2 (2004) E139
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(2004)
PLoS Biol
, vol.2
-
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Amsterdam, A.1
Sadler, K.C.2
Lai, K.3
Farrington, S.4
Bronson, R.T.5
Lees, J.A.6
Hopkins, N.7
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66
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57749187631
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Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency
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This report shows that rpL24 gene haploinsufficiency can suppress cancer progression driven by overexpression of the proto-oncogene c-Myc. This important finding directly implicates Myc's effect on ribosome biogenesis in its ability to increase cell size, independent of its transcriptional effects on known cell-cycle regulators. Furthermore, results reported here show that restoration of protein synthesis to normal levels in Emu-Myc/+ transgenic mice allows for more efficient apoptotic elimination of precancerous cells. Finally, the authors link the oncogenic effect of increased protein synthesis rates in Myc overexpressing mice to a specific deregulation of IRES-dependent translation of Cdk11, which leads to cytokinesis defects and genome instability. This paper thus links a defect in ribosome biogenesis to a specific effect on gene expression with direct consequences for oncogenesis.
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Barna M., Pusic A., Zollo O., Costa M., Kondrashov N., Rego E., Rao P.H., and Ruggero D. Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency. Nature 456 (2008) 971-975. This report shows that rpL24 gene haploinsufficiency can suppress cancer progression driven by overexpression of the proto-oncogene c-Myc. This important finding directly implicates Myc's effect on ribosome biogenesis in its ability to increase cell size, independent of its transcriptional effects on known cell-cycle regulators. Furthermore, results reported here show that restoration of protein synthesis to normal levels in Emu-Myc/+ transgenic mice allows for more efficient apoptotic elimination of precancerous cells. Finally, the authors link the oncogenic effect of increased protein synthesis rates in Myc overexpressing mice to a specific deregulation of IRES-dependent translation of Cdk11, which leads to cytokinesis defects and genome instability. This paper thus links a defect in ribosome biogenesis to a specific effect on gene expression with direct consequences for oncogenesis.
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(2008)
Nature
, vol.456
, pp. 971-975
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Barna, M.1
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