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Volumn 5, Issue , 2014, Pages

PARP13 regulates cellular mRNA post-transcriptionally and functions as a pro-apoptotic factor by destabilizing TRAILR4 transcript

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLY (ADP RIBOSE) POLYMERASE 13; TRANSCRIPTOME; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND RECEPTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND RECEPTOR 4; UNCLASSIFIED DRUG; RNA BINDING PROTEIN; TNFRSF10D PROTEIN, HUMAN; TUMOR NECROSIS FACTOR DECOY RECEPTOR; ZC3HAV1 PROTEIN, HUMAN; ZINC FINGER PROTEIN;

EID: 84923279851     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6362     Document Type: Article
Times cited : (84)

References (47)
  • 1
    • 84882437564 scopus 로고    scopus 로고
    • A systematic analysis of the PARP protein family identifies new functions critical for cell physiology
    • Vyas, S., Chesarone-Cataldo, M., Todorova, T., Huang, Y. H. & Chang, P. A systematic analysis of the PARP protein family identifies new functions critical for cell physiology. Nat. Commun. 4, 2240 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2240
    • Vyas, S.1    Chesarone-Cataldo, M.2    Todorova, T.3    Huang, Y.H.4    Chang, P.5
  • 2
    • 84879730573 scopus 로고    scopus 로고
    • Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform
    • Charron, G., Li, M. M., MacDonald, M. R. & Hang, H. C. Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform. Proc. Natl Acad. Sci. USA 110, 11085-11090 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 11085-11090
    • Charron, G.1    Li, M.M.2    Macdonald, M.R.3    Hang, H.C.4
  • 3
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • Gao, G., Guo, X. & Goff, S. P. Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297, 1703-1706 (2002).
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1    Guo, X.2    Goff, S.P.3
  • 4
    • 84877793134 scopus 로고    scopus 로고
    • Tristetraprolin (TTP): Interactions with mRNA and proteins, and current thoughts on mechanisms of action
    • Brooks, S. A. & Blackshear, P. J. Tristetraprolin (TTP): interactions with mRNA and proteins, and current thoughts on mechanisms of action. Biochim. Biophys. Acta 1829, 666-679 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 666-679
    • Brooks, S.A.1    Blackshear, P.J.2
  • 6
    • 84861305735 scopus 로고    scopus 로고
    • Structure of N-terminal domain of ZAP indicates how a zincfinger protein recognizes complex RNA
    • Chen, S. et al. Structure of N-terminal domain of ZAP indicates how a zincfinger protein recognizes complex RNA. Nat. Struct. Mol. Biol. 19, 430-435 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 430-435
    • Chen, S.1
  • 7
    • 0142060863 scopus 로고    scopus 로고
    • Expression of the zinc-finger antiviral protein inhibits alphavirus replication
    • Bick, M. J. et al. Expression of the zinc-finger antiviral protein inhibits alphavirus replication. J. Virol. 77, 11555-11562 (2003).
    • (2003) J. Virol. , vol.77 , pp. 11555-11562
    • Bick, M.J.1
  • 8
    • 80053144075 scopus 로고    scopus 로고
    • Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation
    • Zhu, Y. et al. Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation. Proc. Natl Acad. Sci. USA 108, 15834-15839 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 15834-15839
    • Zhu, Y.1
  • 9
    • 33846083772 scopus 로고    scopus 로고
    • The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA
    • Guo, X., Ma, J., Sun, J. & Gao, G. The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA. Proc. Natl Acad. Sci. USA 104, 151-156 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 151-156
    • Guo, X.1    Ma, J.2    Sun, J.3    Gao, G.4
  • 10
    • 33847194606 scopus 로고    scopus 로고
    • Inhibition of filovirus replication by the zinc finger antiviral protein
    • Muller, S. et al. Inhibition of filovirus replication by the zinc finger antiviral protein. J. Virol. 81, 2391-2400 (2007).
    • (2007) J. Virol. , vol.81 , pp. 2391-2400
    • Muller, S.1
  • 11
    • 84869216627 scopus 로고    scopus 로고
    • Zinc finger antiviral protein inhibits murine gammaherpesvirus 68 M2 expression and regulates viral latency in cultured cells
    • Xuan, Y., Liu, L., Shen, S., Deng, H. & Gao, G. Zinc finger antiviral protein inhibits murine gammaherpesvirus 68 M2 expression and regulates viral latency in cultured cells. J. Virol. 86, 12431-12434 (2012).
    • (2012) J. Virol. , vol.86 , pp. 12431-12434
    • Xuan, Y.1    Liu, L.2    Shen, S.3    Deng, H.4    Gao, G.5
  • 12
    • 84884747041 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by the host zinc finger antiviral protein
    • Mao, R. et al. Inhibition of hepatitis B virus replication by the host zinc finger antiviral protein. PLoS Pathog. 9, e1003494 (2013).
    • (2013) PLoS Pathog. , vol.9
    • Mao, R.1
  • 13
    • 79953155073 scopus 로고    scopus 로고
    • Analyses of SELEX-derived ZAP-binding RNA aptamers suggest that the binding specificity is determined by both structure and sequence of the RNA
    • Huang, Z., Wang, X. & Gao, G. Analyses of SELEX-derived ZAP-binding RNA aptamers suggest that the binding specificity is determined by both structure and sequence of the RNA. Protein Cell 1, 752-759 (2010).
    • (2010) Protein Cell , vol.1 , pp. 752-759
    • Huang, Z.1    Wang, X.2    Gao, G.3
  • 14
    • 78650310818 scopus 로고    scopus 로고
    • ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses
    • Hayakawa, S. et al. ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. Nat. Immunol. 12, 37-44 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 37-44
    • Hayakawa, S.1
  • 15
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • Leung, A. K. et al. Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol. Cell 42, 489-499 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 489-499
    • Leung, A.K.1
  • 16
    • 84885995929 scopus 로고    scopus 로고
    • Reciprocal inhibition between intracellular antiviral signaling and the RNAi machinery in mammalian cells
    • Seo, G. J. et al. Reciprocal inhibition between intracellular antiviral signaling and the RNAi machinery in mammalian cells. Cell Host Microbe 14, 435-445 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 435-445
    • Seo, G.J.1
  • 17
    • 52649109068 scopus 로고    scopus 로고
    • The TRAIL apoptotic pathway in cancer onset, progression and therapy
    • Johnstone, R. W., Frew, A. J. & Smyth, M. J. The TRAIL apoptotic pathway in cancer onset, progression and therapy. Nat. Rev. Cancer 8, 782-798 (2008).
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 782-798
    • Johnstone, R.W.1    Frew, A.J.2    Smyth, M.J.3
  • 18
    • 0031414749 scopus 로고    scopus 로고
    • The novel receptor TRAIL-R4 induces NF-kappaB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain
    • Degli-Esposti, M. A. et al. The novel receptor TRAIL-R4 induces NF-kappaB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain. Immunity 7, 813-820 (1997).
    • (1997) Immunity , vol.7 , pp. 813-820
    • Degli-Esposti, M.A.1
  • 19
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel, F. C. et al. Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity 12, 611-620 (2000).
    • (2000) Immunity , vol.12 , pp. 611-620
    • Kischkel, F.C.1
  • 20
    • 0033667778 scopus 로고    scopus 로고
    • FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2
    • Sprick, M. R. et al. FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2. Immunity 12, 599-609 (2000).
    • (2000) Immunity , vol.12 , pp. 599-609
    • Sprick, M.R.1
  • 21
    • 33749164762 scopus 로고    scopus 로고
    • Differential inhibition of TRAIL-mediated DR5-DISC formation by decoy receptors 1 and 2
    • Merino, D. et al. Differential inhibition of TRAIL-mediated DR5-DISC formation by decoy receptors 1 and 2. Mol. Cell. Biol. 26, 7046-7055 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7046-7055
    • Merino, D.1
  • 22
    • 13144265771 scopus 로고    scopus 로고
    • A novel receptor for Apo2L/TRAIL contains a truncated death domain
    • Marsters, S. A. et al. A novel receptor for Apo2L/TRAIL contains a truncated death domain. Curr. Biol. 7, 1003-1006 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 1003-1006
    • Marsters, S.A.1
  • 23
    • 0037273848 scopus 로고    scopus 로고
    • Apo2L/TRAIL and its death and decoy receptors
    • LeBlanc, H. N. & Ashkenazi, A. Apo2L/TRAIL and its death and decoy receptors. Cell Death Differ. 10, 66-75 (2003).
    • (2003) Cell Death Differ. , vol.10 , pp. 66-75
    • Leblanc, H.N.1    Ashkenazi, A.2
  • 24
    • 79952630372 scopus 로고    scopus 로고
    • Chemotherapy overcomes TRAIL-R4-mediated TRAIL resistance at the DISC level
    • Morizot, A. et al. Chemotherapy overcomes TRAIL-R4-mediated TRAIL resistance at the DISC level. Cell Death Differ. 18, 700-711 (2011).
    • (2011) Cell Death Differ. , vol.18 , pp. 700-711
    • Morizot, A.1
  • 25
    • 84880676846 scopus 로고    scopus 로고
    • Zinc-finger antiviral protein mediates retinoic acid inducible gene I-like receptor-independent antiviral response to murine leukemia virus
    • Lee, H. et al. Zinc-finger antiviral protein mediates retinoic acid inducible gene I-like receptor-independent antiviral response to murine leukemia virus. Proc. Natl Acad. Sci. USA 110, 12379-12384 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 12379-12384
    • Lee, H.1
  • 26
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W., Sherman, B. T. & Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 27
    • 27344435774 scopus 로고    scopus 로고
    • Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles
    • Subramanian, A. et al. Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc. Natl Acad. Sci. USA 102, 15545-15550 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15545-15550
    • Subramanian, A.1
  • 28
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • Schoggins, J. W. & Rice, C. M. Interferon-stimulated genes and their antiviral effector functions. Curr. Opin. Virol. 1, 519-525 (2011).
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 29
    • 10944239669 scopus 로고    scopus 로고
    • Induction of IFN-regulated factors and antitumoral surveillance by transfected placebo plasmid DNA
    • Li, S. et al. Induction of IFN-regulated factors and antitumoral surveillance by transfected placebo plasmid DNA. Mol. Ther. 11, 112-119 (2005).
    • (2005) Mol. Ther. , vol.11 , pp. 112-119
    • Li, S.1
  • 30
    • 84858446718 scopus 로고    scopus 로고
    • Regulation of cytoplasmic mRNA decay
    • Schoenberg, D. R. & Maquat, L. E. Regulation of cytoplasmic mRNA decay. Nat. Rev. Genet. 13, 246-259 (2012).
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 246-259
    • Schoenberg, D.R.1    Maquat, L.E.2
  • 32
    • 11844278458 scopus 로고    scopus 로고
    • Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets
    • Lewis, B. P., Burge, C. B. & Bartel, D. P. Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets. Cell 120, 15-20 (2005).
    • (2005) Cell , vol.120 , pp. 15-20
    • Lewis, B.P.1    Burge, C.B.2    Bartel, D.P.3
  • 33
    • 84875508430 scopus 로고    scopus 로고
    • MicroRNAs involved in skeletal muscle differentiation
    • Luo, W., Nie, Q. & Zhang, X. MicroRNAs involved in skeletal muscle differentiation. J. Genet. Genomics 40, 107-116 (2013).
    • (2013) J. Genet. Genomics , vol.40 , pp. 107-116
    • Luo, W.1    Nie, Q.2    Zhang, X.3
  • 34
    • 82055164092 scopus 로고    scopus 로고
    • ViennaRNA package 2.0
    • Lorenz, R. et al. ViennaRNA package 2.0. Algorithms Mol. Biol. 6, 26 (2011).
    • (2011) Algorithms Mol. Biol. , vol.6 , pp. 26
    • Lorenz, R.1
  • 35
    • 33750221973 scopus 로고    scopus 로고
    • Effects of Dicer and Argonaute down-regulation on mRNA levels in human HEK293 cells
    • Schmitter, D. et al. Effects of Dicer and Argonaute down-regulation on mRNA levels in human HEK293 cells. Nucleic Acids Res. 34, 4801-4815 (2006).
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4801-4815
    • Schmitter, D.1
  • 36
    • 37849033506 scopus 로고    scopus 로고
    • Biochemical analysis of the native TRAIL death-inducing signaling complex
    • Walczak, H. & Haas, T. L. Biochemical analysis of the native TRAIL death-inducing signaling complex. Methods Mol. Biol. 414, 221-239 (2008).
    • (2008) Methods Mol. Biol. , vol.414 , pp. 221-239
    • Walczak, H.1    Haas, T.L.2
  • 37
    • 84886948521 scopus 로고    scopus 로고
    • TRAIL on trial: Preclinical advances in cancer therapy
    • Stuckey, D. W. & Shah, K. TRAIL on trial: preclinical advances in cancer therapy. Trends Mol. Med. 19, 685-694 (2013).
    • (2013) Trends Mol. Med. , vol.19 , pp. 685-694
    • Stuckey, D.W.1    Shah, K.2
  • 38
    • 84905407213 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase inhibitors sensitize cancer cells to death receptor-mediated apoptosis by enhancing death receptor expression
    • Meng, X. W. et al. Poly(ADP-ribose) polymerase inhibitors sensitize cancer cells to death receptor-mediated apoptosis by enhancing death receptor expression. J. Biol. Chem. 289, 20543-20558 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 20543-20558
    • Meng, X.W.1
  • 39
    • 84864378884 scopus 로고    scopus 로고
    • New PARP gene with an anti-alphavirus function
    • Atasheva, S., Akhrymuk, M., Frolova, E. I. & Frolov, I. New PARP gene with an anti-alphavirus function. J. Virol. 86, 8147-8160 (2012).
    • (2012) J. Virol. , vol.86 , pp. 8147-8160
    • Atasheva, S.1    Akhrymuk, M.2    Frolova, E.I.3    Frolov, I.4
  • 40
    • 84907211041 scopus 로고    scopus 로고
    • PARP12, an interferon stimulated gene involved in the control of protein translation and inflammation
    • Welsby, I. et al. PARP12, an interferon stimulated gene involved in the control of protein translation and inflammation. J. Biol. Chem. 289, 26642-26657 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 26642-26657
    • Welsby, I.1
  • 41
    • 79551647673 scopus 로고    scopus 로고
    • Genome-wide identification of Ago2 binding sites from mouse embryonic stem cells with and without mature microRNAs
    • Leung, A. K. et al. Genome-wide identification of Ago2 binding sites from mouse embryonic stem cells with and without mature microRNAs. Nat. Struct. Mol. Biol. 18, 237-244 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 237-244
    • Leung, A.K.1
  • 42
    • 4544242734 scopus 로고    scopus 로고
    • Death induction by recombinant native TRAIL and its prevention by a caspase 9 inhibitor in primary human esophageal epithelial cells
    • Kim, S. H. et al. Death induction by recombinant native TRAIL and its prevention by a caspase 9 inhibitor in primary human esophageal epithelial cells. J. Biol. Chem. 279, 40044-40052 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 40044-40052
    • Kim, S.H.1
  • 43
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak, K. J. & Schmittgen, T. D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25, 402-408 (2001).
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 44
    • 84880841239 scopus 로고    scopus 로고
    • Synthesis and labeling of RNA in vitro
    • Chapter 4, Unit 4.
    • Huang, C. & Yu, Y. T. Synthesis and labeling of RNA in vitro. Curr. Protoc. Mol. Biol. Chapter 4, Unit 4.15 (2013).
    • (2013) Curr. Protoc. Mol. Biol. , pp. 15
    • Huang, C.1    Yu, Y.T.2
  • 45
    • 84881539278 scopus 로고    scopus 로고
    • Metabolic labeling of newly transcribed RNA for high resolution gene expression profiling of RNA synthesis, processing and decay in cell culture
    • Radle, B. et al. Metabolic labeling of newly transcribed RNA for high resolution gene expression profiling of RNA synthesis, processing and decay in cell culture. J. Vis. Exp. 78, e50195 (2013).
    • (2013) J. Vis. Exp. , vol.78
    • Radle, B.1
  • 46
    • 57749180679 scopus 로고    scopus 로고
    • Messenger RNA half-life measurements in mammalian cells
    • Chen, C. Y., Ezzeddine, N. & Shyu, A. B. Messenger RNA half-life measurements in mammalian cells. Methods Enzymol. 448, 335-357 (2008).
    • (2008) Methods Enzymol. , vol.448 , pp. 335-357
    • Chen, C.Y.1    Ezzeddine, N.2    Shyu, A.B.3
  • 47
    • 0346564424 scopus 로고    scopus 로고
    • Real-time RT-PCR analysis of mRNA decay: Half-life of Beta-actin mRNA in human leukemia CCRF-CEM and Nalm-6 cell lines
    • Leclerc, G. J., Leclerc, G. M. & Barredo, J. C. Real-time RT-PCR analysis of mRNA decay: half-life of Beta-actin mRNA in human leukemia CCRF-CEM and Nalm-6 cell lines. Cancer Cell Int. 2, 1 (2002).
    • (2002) Cancer Cell Int. , vol.2 , pp. 1
    • Leclerc, G.J.1    Leclerc, G.M.2    Barredo, J.C.3


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