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April 17th, 2025
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Laboratoire de Biologie et Modelisation de la Cellule, Ecole Normale Superieure - Lyon, Universite Claude Bernard Lyon, U1293, UMR5239, France
molecular biology
biorxiv

Retroviral adapters hijack the RNA helicase UPF1 in a CRM1/XPO1 dependent manner and reveal proviral roles of UPF1.

Prochasson, L.Open in Google Scholar•Mghezzi-Habellah, M.Open in Google Scholar•Roisin, A.Open in Google Scholar•Palma, M.Open in Google Scholar•Robin, J.-P.Open in Google Scholar•de Bossoreille, S.Open in Google Scholar•Cluet, D.Open in Google Scholar•Mouehli, M.Open in Google Scholar•Decimo, D.Open in Google Scholar•Desrames, A.Open in Google Scholaret al.

The hijacking of CRM1 export is an important step of the retroviral replication cycle. Here, we investigated the consequences of this hijacking for the host. During HTLV-1 infection, we identified that this hijacking by the viral protein Rex favours the association between CRM1 and the RNA helicase UPF1, leading to a decreased affinity of UPF1 for cellular RNA and its nuclear retention. As a consequence, we found that the nonsense mediated mRNA decay (NMD), known to have an antiviral function, was inhibited. Corroborating these results, we described a similar process with Rev, the functional homolog of Rex from HIV-1. Unexpectedly, we also found that, for HTLV-1 , this process is coupled with the specific loading of UPF1 onto vRNA, independently of NMD. In this latter context, UPF1 positively regulates several steps of the viral replication cycle, from the nuclear export of vRNA to the production of mature viral particles.

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