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Volumn 19, Issue 12, 2012, Pages 1282-1286

Noncanonical G recognition mediates KSRP regulation of let-7 biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

KSRP PROTEIN; MICRORNA; PROTEIN; UNCLASSIFIED DRUG;

EID: 84870824218     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2427     Document Type: Article
Times cited : (39)

References (32)
  • 2
    • 77955902024 scopus 로고    scopus 로고
    • The widespread regulation of microRNA biogenesis, function and decay
    • Krol, J., Loedige, I. & Filipowicz, W. The widespread regulation of microRNA biogenesis, function and decay. Nat. Rev. Genet. 11, 597-610 (2010).
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 597-610
    • Krol, J.1    Loedige, I.2    Filipowicz, W.3
  • 3
    • 55049119136 scopus 로고    scopus 로고
    • Posttranscriptional regulation of miRNAs harboring conserved terminal loops
    • Michlewski, G., Guil, S., Semple, C.A. & Cáceres, J.F. Posttranscriptional regulation of miRNAs harboring conserved terminal loops. Mol. Cell 32, 383-393 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 383-393
    • Michlewski, G.1    Guil, S.2    Semple, C.A.3    Cáceres, J.F.4
  • 4
    • 50549095181 scopus 로고    scopus 로고
    • Let-7 microRNAs in development, stem cells and cancer
    • Büssing, I., Slack, F.J. & Grosshans, H. Let-7 microRNAs in development, stem cells and cancer. Trends Mol. Med. 14, 400-409 (2008).
    • (2008) Trends Mol. Med. , vol.14 , pp. 400-409
    • Büssing, I.1    Slack, F.J.2    Grosshans, H.3
  • 5
    • 40849108663 scopus 로고    scopus 로고
    • Selective blockade of microRNA processing by Lin28
    • Viswanathan, S.R., Daley, G.Q. & Gregory, R.I. Selective blockade of microRNA processing by Lin28. Science 320, 97-100 (2008).
    • (2008) Science , vol.320 , pp. 97-100
    • Viswanathan, S.R.1    Daley, G.Q.2    Gregory, R.I.3
  • 6
    • 68749102148 scopus 로고    scopus 로고
    • TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation
    • Heo, I. et al. TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation. Cell 138, 696-708 (2009).
    • (2009) Cell , vol.138 , pp. 696-708
    • Heo, I.1
  • 7
    • 70349820140 scopus 로고    scopus 로고
    • Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells
    • Hagan, J.P., Piskounova, E. & Gregory, R.I. Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells. Nat. Struct. Mol. Biol. 16, 1021-1025 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1021-1025
    • Hagan, J.P.1    Piskounova, E.2    Gregory, R.I.3
  • 8
    • 77955425756 scopus 로고    scopus 로고
    • Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis
    • Michlewski, G. & Cáceres, J.F. Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis. Nat. Struct. Mol. Biol. 17, 1011-1018 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1011-1018
    • Michlewski, G.1    Cáceres, J.F.2
  • 9
    • 67649277689 scopus 로고    scopus 로고
    • The RNA-binding protein KSRP promotes the biogenesis of a subset of microRNAs
    • Trabucchi, M. et al. The RNA-binding protein KSRP promotes the biogenesis of a subset of microRNAs. Nature 459, 1010-1014 (2009).
    • (2009) Nature , vol.459 , pp. 1010-1014
    • Trabucchi, M.1
  • 10
    • 84855421472 scopus 로고    scopus 로고
    • Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28
    • Loughlin, F.E. et al. Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28. Nat. Struct. Mol. Biol. 19, 84-89 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 84-89
    • Loughlin, F.E.1
  • 11
    • 81855228621 scopus 로고    scopus 로고
    • Molecular basis for interaction of let-7 microRNAs with Lin28
    • Nam, Y., Chen, C., Gregory, R.I., Chou, J.J. & Sliz, P. Molecular basis for interaction of let-7 microRNAs with Lin28. Cell 147, 1080-1091 (2011).
    • (2011) Cell , vol.147 , pp. 1080-1091
    • Nam, Y.1    Chen, C.2    Gregory, R.I.3    Chou, J.J.4    Sliz, P.5
  • 13
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde, R., Edwards, L. & Regan, L. Structure and function of KH domains. FEBS J. 275, 2712-2726 (2008).
    • (2008) FEBS J. , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 14
    • 52649112259 scopus 로고    scopus 로고
    • The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
    • García-Mayoral, M.F., Díaz-Moreno, I., Hollingworth, D. & Ramos, A. The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets. Nucleic Acids Res. 36, 5290-5296 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5290-5296
    • García-Mayoral, M.F.1    Díaz-Moreno, I.2    Hollingworth, D.3    Ramos, A.4
  • 15
    • 84864959576 scopus 로고    scopus 로고
    • KH domains with impaired nucleic acid binding as a tool for functional analysis
    • Hollingworth, D. et al. KH domains with impaired nucleic acid binding as a tool for functional analysis. Nucleic Acids Res. 40, 6873-6886 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 6873-6886
    • Hollingworth, D.1
  • 16
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome
    • Lewis, H.A. et al. Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome. Cell 100, 323-332 (2000).
    • (2000) Cell , vol.100 , pp. 323-332
    • Lewis, H.A.1
  • 17
    • 21744454842 scopus 로고    scopus 로고
    • X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids
    • Backe, P.H., Messias, A.C., Ravelli, R.B., Sattler, M. & Cusack, S. X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids. Structure 13, 1055-1067 (2005).
    • (2005) Structure , vol.13 , pp. 1055-1067
    • Backe, P.H.1    Messias, A.C.2    Ravelli, R.B.3    Sattler, M.4    Cusack, S.5
  • 18
    • 34047269428 scopus 로고    scopus 로고
    • The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation
    • García-Mayoral, M.F. et al. The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation. Structure 15, 485-498 (2007).
    • (2007) Structure , vol.15 , pp. 485-498
    • García-Mayoral, M.F.1
  • 19
    • 0026611261 scopus 로고
    • Preparation of 13C and 15N labelled RNAs for heteronuclear multi-dimensional NMR studies
    • Nikonowicz, E.P. et al. Preparation of 13C and 15N labelled RNAs for heteronuclear multi-dimensional NMR studies. Nucleic Acids Res. 20, 4507-4513 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4507-4513
    • Nikonowicz, E.P.1
  • 20
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 21
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 22
    • 0343459675 scopus 로고
    • The program XEASY for computer supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T., Billeter, M., Guntert, P. & Wuthrich, K. The program XEASY for computer supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6, 1-10 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Guntert, P.4    Wuthrich, K.5
  • 23
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge, J.P., Habeck, M., Rieping, W. & Nilges, M. ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 19, 315-316 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 25
    • 0035798243 scopus 로고    scopus 로고
    • Structural basis for recognition of the intron branch site RNA by splicing factor 1
    • Liu, Z. et al. Structural basis for recognition of the intron branch site RNA by splicing factor 1. Science 294, 1098-1102 (2001).
    • (2001) Science , vol.294 , pp. 1098-1102
    • Liu, Z.1
  • 26
    • 0031160103 scopus 로고    scopus 로고
    • Temperature dependence of 1 H chemical shifts in proteins
    • Baxter, N.J. & Williamson, M.P. Temperature dependence of 1 H chemical shifts in proteins. J. Biomol. NMR 9, 359-369 (1997).
    • (1997) J. Biomol. NMR , vol.9 , pp. 359-369
    • Baxter, N.J.1    Williamson, M.P.2
  • 27
    • 0036386164 scopus 로고    scopus 로고
    • Hydrogen bonds in human ubiquitin reflected in temperature coefficients of amide protons
    • Cierpicki, T., Zhukov, I., Byrd, R.A. & Otlewski, J. Hydrogen bonds in human ubiquitin reflected in temperature coefficients of amide protons. J. Magn. Reson. 157, 178-180 (2002).
    • (2002) J. Magn. Reson. , vol.157 , pp. 178-180
    • Cierpicki, T.1    Zhukov, I.2    Byrd, R.A.3    Otlewski, J.4
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 29-32 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 29
    • 52649112259 scopus 로고    scopus 로고
    • The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
    • García-Mayoral, M.F., Díaz-Moreno, I., Hollingworth, D. & Ramos, A. The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets. Nucleic Acids Res. 36, 5290-5296 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5290-5296
    • García-Mayoral, M.F.1    Díaz-Moreno, I.2    Hollingworth, D.3    Ramos, A.4
  • 30
    • 0034351982 scopus 로고    scopus 로고
    • Enhancement by Mg2+ of domain specificity in Ca2+-dependent interactions of calmodulin with target sequences
    • Martin, S.R., Masino, L. & Bayley, P.M. Enhancement by Mg2+ of domain specificity in Ca2+-dependent interactions of calmodulin with target sequences. Protein Sci. 9, 2477-2488 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 2477-2488
    • Martin, S.R.1    Masino, L.2    Bayley, P.M.3
  • 31
    • 77956339799 scopus 로고    scopus 로고
    • Molecular basis of FIR-mediated c-myc transcriptional control
    • Cukier, C.D. et al. Molecular basis of FIR-mediated c-myc transcriptional control. Nat. Struct. Mol. Biol. 17, 1058-1064 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1058-1064
    • Cukier, C.D.1
  • 32
    • 84857052573 scopus 로고    scopus 로고
    • PI3K/AKT signaling determines a switch between distinct KSRP functions favoring skeletal miogenesis
    • Briata, P. et al. PI3K/AKT signaling determines a switch between distinct KSRP functions favoring skeletal miogenesis. Cell Death Differ. 19, 478-487 (2012).
    • (2012) Cell Death Differ. , vol.19 , pp. 478-487
    • Briata, P.1


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