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Boutoual, R.

Publications and source records attributed to Boutoual, R..

2 recordsLinked to original sources

Constitutive cGAS-STING activation in ALT+ cells

Stimulator of interferon genes (STING) is a pivotal mediator of anti-tumor immunity, activated downstream of cytoplasmic DNA recognition by cyclic GMP-AMP synthase (cGAS). In cells that employ the alternative lengthening of telomeres (ALT) pathway, extrachromosomal telomeric repeats (ECTRs) act as potent activators of the cGAS-STING pathway. Although ALT+ cells were previously thought to evade this pathway through epigenetic silencing, our findings reveal more nuanced adaptive mechanisms that involve the spatial regulation of STING and the clearance of immunostimulatory ECTR species. In the vast majority of ALT+ cells, ongoing ECTR production drives sustained 2'3'-cGAMP synthesis, directing STING to the Golgi apparatus for immune signaling before lysosomal degradation. Lysosomal degradation of STING relies largely on interferon regulatory factor 3 (IRF3), with minimal involvement of TANK-binding kinase 1 (TBK1), pointing at a novel role for IRF3 in STING trafficking in ALT+ cells. Another adaptive mechanism involves the removal of immunogenic cytoplasmic ECTRs through STING-mediated lysosomal degradation. These mechanisms likely cooperate to restrict chronic interferon signaling that might otherwise prevent ALT+ cancers from emerging. These findings refine our understanding of immune sensing in ALT+ cancers, revealing how ALT+ cells respond to continuous ECTR production and suggesting a potential therapeutic target to modulate the microenvironment of ALT+ tumors.

cell biology↗

Human Elp3/Kat9 is a mitochondrial tRNA modifying enzyme

Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent deacetylase sirtuin 3 (SIRT3), however it remains unclear whether corresponding mitochondrial acetyltransferases exist. We used a bioinformatics approach to search for mitochondrial proteins with an acetyltransferase catalytic domain, and identified a novel splice variant of ELP3 (mt-ELP3) of the elongator complex, which localizes to the mitochondrial matrix in mammalian cells. Unexpectedly, mt-ELP3 does not mediate mitochondrial protein acetylation but instead induces a post-transcriptional modification of mitochondrial-transfer RNAs (mt-tRNAs). Overexpression of mt-ELP3 leads to the protection of mt-tRNAs against the tRNA-specific RNase angiogenin, increases mitochondrial translation, and furthermore increases expression of OXPHOS complexes. This study thus identifies mt-ELP3 as a non-canonical mt-tRNA modifying enzyme.

molecular biology↗