Role of GW182 proteins in miRNA-mediated gene silencing

• Applicant: Dr. Elisa Izaurralde (†)
• Subject Area: Cell Biology
• Term: from 2007 to 2014
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 33442413

Final Report Abstract

No abstract available

Publications

• (2011), GW182 proteins recruit cytoplasmic deadenylase complexes to miRNA targets, Mol Cell 44:120-133
  Braun JE, Huntzinger E, Fauser M, Izaurralde E
  (See online at https://doi.org/10.1016/j.molcel.2011.09.007)
• (2012), A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation, Nat Struct Mol Biol 19:1324–1331
  Braun JE, Truffault V, Boland A, Huntzinger E, Chang CT, Haas G, Weichenrieder O, Coles M, Izaurralde E
  (See online at https://doi.org/10.1038/nsmb.2413)
• (2012), The Caenorhabditis elegans GW182 protein AIN-1 interacts with PAB-1 and subunits of the PAN2-PAN3 and CCR4-NOT deadenylase complexes, Nucleic Acids Res 40:5651-5665
  Kuzuoglu-Öztürk D, Huntzinger E, Schmidt S, Izaurralde E
  (See online at https://doi.org/10.1093/nar/gks218)
• (2012), The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex, Nucleic Acids Res 40:11058-11072
  Petit AP, Wohlbold L, Bawankar P, Huntzinger E, Schmidt S, Izaurralde E, Weichenrieder O
  (See online at https://doi.org/10.1093/nar/gks883)
• (2013), An unusual arrangement of two 14-3-3 domains in the SMG5-SMG7 heterodimer is required for efficient nonsense-mediated mRNA decay, Genes Dev 27:211-225
  Jonas S, Weichenrieder O, Izaurralde E
  (See online at https://doi.org/10.1101/gad.206672.112)
• (2013), GW182 proteins cause PABP dissociation from silenced miRNA targets in the absence of deadenylation, EMBO J 32:1052-1065
  Zekri L, Kuzuoğlu-Öztürk D, Izaurralde E
  (See online at https://doi.org/10.1038/emboj.2013.44)
• (2013), miRISC recruits decapping factors to miRNA targets to enhance their degradation, Nucleic Acids Res 41:8692–8705
  Nishihara T, Zekri L, Braun JE, Izaurralde E
  (See online at https://doi.org/10.1093/nar/gkt619)
• (2013), NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain, RNA Biol 10:228-244
  Bawankar P, Loh B, Wohlbold L, Schmidt S, Izaurralde E
  (See online at https://doi.org/10.4161/rna.23018)
• (2013), Structure and assembly of the NOT module of the human CCR4-NOT complex, Nat Struct Mol Biol 20:1289–1297
  Boland A, Chen Y, Raisch T, Jonas S, Kuzuoğlu-Öztürk D, Wohlbold L, Weichenrieder O, Izaurralde E
  (See online at https://doi.org/10.1038/nsmb.2681)
• (2013), Structure of the PAN3 Pseudokinase Reveals the Basis for Interactions with the PAN2 Deadenylase and the GW182 Proteins, Mol Cell 51:360-373
  Christie M, Boland A, Huntzinger E, Weichenrieder O, Izaurralde E
  (See online at https://doi.org/10.1016/j.molcel.2013.07.011)
• (2013), The interactions of GW182 proteins with PABP and deadenylases are required for both translational repression and degradation of miRNA targets, Nucleic Acids Res 41:978-994
  Huntzinger E, Kuzuoğlu-Öztürk D, Braun JE, Eulalio A, Wohlbold L, Izaurralde E
  (See online at https://doi.org/10.1093/nar/gks1078)
• (2013), The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2, Genes Dev 27:2125–2138
  Loh B, Jonas S, Izaurralde E
  (See online at https://doi.org/10.1101/gad.226951.113)
• (2014), A DDX6-NOT1 complex and W-binding pockets in CNOT9 reveal direct links between miRNA target recognition and silencing, Mol Cell 54:737-750
  Chen Y, Boland A, Kuzuoğlu-Öztürk D, Bawankar P, Loh B, Chang CT, Weichenrieder O, Izaurralde E
  (See online at https://doi.org/10.1016/j.molcel.2014.03.034)
• (2014), Structural basis for the Nanosmediated recruitment of the CCR4-NOT complex and translational repression, Genes Dev 28:888–901
  Bhandari D, Raisch T, Weichenrieder O, Jonas S, Izaurralde E
  (See online at https://doi.org/10.1101/gad.237289.113)
• (2014), The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1, Nucleic Acids Res 42:5217–5233
  Chang CT, Bercovich N, Loh B, Jonas S, Izaurralde E
  (See online at https://doi.org/10.1093/nar/gku129)