Société Française de Biochimie et Biologie Moléculaire

Pauline Herviou - OCTOBER 2020

Paris Institute of Technology for Life, Food and Environmental Sciences "hnRNP H/F drive RNA G-quadruplex-mediated translation linked to genomic instability and therapy resistance in glioblastoma" Nature Communications, 11, 2661 (2020).
Herviou, P.*, Le Bras, M.*, Dumas, L., Hieblot, C., Gilhodes, J., Cioci, G., Hugnot, J.P., Ameadan, A., Guillonneau, F., Dassi, E., Cammas, A. and Millevoi, S.

Pauline Herviou, 26 years old, obtained an engineering degree with the specialty biotechnologies in 2018 at AgroParisTech (Paris Institute of Technology for Life, Food and Environmental Sciences). She is now performing a doctorate under the supervision of Anne Cammas and Stefania Millevoi at the Cancer Research Center of Toulouse (CRCT). Her work focuses on the function of RNA G-quadruplexes in mRNA translation. Recent transcriptome-wide studies suggested that, in cells, the equilibrium between folded and unfolded G-quadruplexes is tightly regulated. In the recent Nature communication issue, Pauline Herviou and collaborators identified the RNA binding proteins hnRNP H/F as important components of the machinery that maintains RNA G-quadruplexes in an unfolded state. Further investigation revealed their function in translational control of RNA G-quadruplex-containing mRNAs involved in the maintenance of genome integrity and in the cell response to stress. Finally, in agreement with these results, their work underscored a role for hnRNP H/F in therapy resistance in glioblastoma, one of the deadliest forms of brain cancer.


Cancer Research Center of Toulouse (CRCT)

TEAM "RNA-binding proteins and post-transcriptional regulation in cancer" UMR1037
2 avenue Hubert Curien



This email address is being protected from spambots. You need JavaScript enabled to view it.


Article Summury:

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.