Journal
NATURE COMMUNICATIONS
Volume 11, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-020-16168-x
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Funding
- FEDER through the Operational Programme for Competitiveness Factors and employment 2007-2013
- Canceropole Ile de France
- INSERM, Universite Toulouse III -Paul Sabatier, CNRS
- LNCC (Ligue Nationale Contre le Cancer)
- ARC (Association pour la Recherche contre le Cancer)
- Laboratoire d'Excellence TOUCAN [ANR11-LABX]
- ANR [ANR-17-CE120017-01, ANR-17-CE12-0017-01]
- Midi-Pyrenees Region/INSERM
- MENRT
- Emergence Canceropole GSO
- Agence Nationale de la Recherche (ANR) [ANR-17-CE12-0017] Funding Source: Agence Nationale de la Recherche (ANR)
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RNA G-quadruplexes (RG4s) are four-stranded structures known to control mRNA translation of cancer relevant genes. RG4 formation is pervasive in vitro but not in cellulo, indicating the existence of poorly characterized molecular machinery that remodels RG4s and maintains them unfolded. Here, we performed a quantitative proteomic screen to identify cytosolic proteins that interact with a canonical RG4 in its folded and unfolded conformation. Our results identified hnRNP H/F as important components of the cytoplasmic machinery modulating the structural integrity of RG4s, revealed their function in RG4-mediated translation and uncovered the underlying molecular mechanism impacting the cellular stress response linked to the outcome of glioblastoma. RNA G-quadruplexes (RG4s) have been functionally linked to cancer gene expression. Here, Herviou, Le Bras et al. have identified the protein machinery modulating RG4s and reveal the role and mechanism of hnRNP H/F and DHX36 in RG4-mediated translational regulation affecting cancer treatment in glioblastoma.
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