Mathieu Quesnel-Vallières

@rna-ken.bsky.social

Cancer, immunotherapy & RNA splicing researcher Assistant Professor, Department of Immunology and Cell Biology, Université de Sherbrooke https://mqvlab.com

As always, the RiboClub meeting has an excellent line-up of speakers this year. There are also generous travel awards still available for trainees and ECRs. Deadline is coming up this Sunday, July 27!

@riboclub.bsky.social · 3w ago

Great news! Early-bird registration, abstract submission, and travel fellowship application deadlines for the 27th RiboClub Annual Meeting have been extended to Sunday, July 27, 2026. home.riboclub.org/annual-meeti...

RNA Canada ARN is excited to be at the 2026 RNA Society Meeting. We will be set up at a table in the exhibition hall! Stop by to talk with RNA Canada members, grab some free swag, and sign up to renew your membership. !

I just described one of my aims as being "functional with translational undercurrents" in a grant that I'm writing, as if I were describing a fine wine, and for this sole reason I already consider this application to be successful.

New paper: More than 2700 human 3′UTRs are highly conserved. These 3′UTRs are essential components in mRNA templates, as their deletion decreases protein activity without changing protein abundance. Highly conserved 3′UTRs help the folding of proteins with long IDRs. www.biorxiv.org/content/10.1...

mRNA 3′UTRs chaperone intrinsically disordered regions to control protein activity

More than 2,700 human mRNA 3′UTRs have hundreds of highly conserved (HC) nucleotides, but their biological roles are unclear. Here, we show that mRNAs with HC 3′UTRs mostly encode proteins with long intrinsically disordered regions (IDRs), including MYC, UTX, and JMJD3. These proteins are only fully active when translated from mRNA templates that include their 3′UTRs, raising the possibility of functional interactions between 3′UTRs and IDRs. Rather than affecting protein abundance or localization, we find that HC 3′UTRs control transcriptional or histone demethylase activity through co-translationally determined protein oligomerization states that are kinetically stable. 3′UTR-dependent changes in protein folding require mRNA-IDR interactions, suggesting that mRNAs act as IDR chaperones. These mRNAs are multivalent, a biophysical RNA feature that enables their translation in network-like condensates, which provide favorable folding environments for proteins with long IDRs. These data indicate that the coding sequence is insufficient for the biogenesis of biologically active conformations of IDR-containing proteins and that RNA can catalyze protein folding. ### Competing Interest Statement The authors have declared no competing interest. Pershing Square Foundation, https://ror.org/04tce9s05 G. Harold & Leila Y. Mathers Foundation National Institutes of Health, DP1GM123454, R35GM144046 Memorial Sloan Kettering Cancer Center, https://ror.org/02yrq0923, P30 CA008748

biorxiv.org

dFORCE provides a revised timeline for mRNA synthesis wherein cleavage, termination, and m6A deposition occur earlier than, or at least partially decoupled from, the bulk of splicing in thousands of genes

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