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Raynaud, N.

Publications and source records attributed to Raynaud, N..

2 recordsLinked to original sources

The E. coli CNF1 toxin induces fetal reprogramming of intestinal stem cells and a serrated colorectal cancer transcriptional signature in organoids

Mechanistic insights are essential to understand how gut microbiota pathobionts contribute to tumorigenesis, given the mounting evidence linking them to colorectal cancer. We report a higher prevalence of the Rho GTPases-targeting cnf1 toxin gene from Escherichia coli in the microbiota of early-stage, proximal colorectal cancer. Comparative gene set enrichment analysis reveals a concordant serrated pathway signature between colorectal cancer tissue of patients colonized with cnf1+ bacteria and CNF1-treated mouse intestinal organoids. RNA sequencing of organoids shows that CNF1 induces a fetal-like transcriptional reprogramming. Using integrated approaches, we demonstrate that CNF1 reprograms Lgr5 stem cells into a Ly6a/Sca-1 fetal-like state, that exhibits enhanced stemness potential. This reprogramming is preceded by a Yap/Taz-driven early transcriptional program and nuclear translocation of Yap. Functional analyses identify a RhoA/Rock-Yap/Taz-dependent transition to Ly6a/Sca-1 stem cells, highlighting a mechanistic link between bacterial effectors and stem cell plasticity in colorectal tumorigenesis.

cancer biology↗

Ashwin and FAM98 paralogs define nuclear and cytoplasmic RNA ligase complexes for tRNA biogenesis and the unfolded protein response

The tRNA ligase complex (tRNA-LC) seals tRNA exon halves in the nucleus after the removal of a single intron, and joins XBP1-mRNA exons in the cytoplasm as part of the unfolded protein response (UPR). This dual function requires simultaneous nuclear and cytoplasmic localization. Here, we reveal that Ashwin (ASW), the vertebrate-specific subunit of the tRNA-LC, serves as its nuclear import factor. ASW displays a dual nuclear localisation signal (NLS) which, upon disruption, leads to the retention of the tRNA-LC in the cytoplasm with a consequent impairment of pre-tRNA splicing and accumulation of 5 tRNA fragments. We also show that the tRNA-LC exists in three forms depending on which FAM98 paralog is chosen, either FAM98A, FAM98B or FAM98C. We find that ASW interacts exclusively with the FAM98B-containing complex, allowing its nuclear localization for tRNA biogenesis. Attaching an NLS to RTCB, the catalytic and indispensable subunit, rescues pre-tRNA splicing in cells depleted of ASW. We envision that vertebrates evolved ASW to localize a sub-population of tRNA-LC to the nucleus, while using FAM98 paralogs to retain a fraction of RTCB in the cytoplasm for XBP1-mRNA splicing during UPR.

cell biology↗