Proteomics

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HnRNP 1 H/F drive RNA G-quadruplex-mediated translation linked to genomic instability and therapy resistance in glioblastoma


ABSTRACT: 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 a poorly characterized molecular machinery that remodels RG4s and maintains them unfolded. To help fill this gap in knowledge, 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 RG4s structural integrity, revealed their function in RG4-mediated translation and uncovered the underlying molecular mechanism impacting cellular stress response linked to the outcome of glioblastoma, one of the deadliest types of solid cancer overall.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

DISEASE(S): Brain Glioblastoma Multiforme,Brain Cancer

SUBMITTER: François GUILLONNEAU  

LAB HEAD: Stefania Millevoi

PROVIDER: PXD015609 | Pride | 2020-11-11

REPOSITORIES: Pride

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hnRNP H/F drive RNA G-quadruplex-mediated translation linked to genomic instability and therapy resistance in glioblastoma.

Herviou Pauline P   Le Bras Morgane M   Dumas Leïla L   Hieblot Corinne C   Gilhodes Julia J   Cioci Gianluca G   Hugnot Jean-Philippe JP   Ameadan Alfred A   Guillonneau François F   Dassi Erik E   Cammas Anne A   Millevoi Stefania S  

Nature communications 20200527 1


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 componen  ...[more]

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