bioRxiv Science⌕ Search

Biology subjects

Sulova, M.

Publications and source records attributed to Sulova, M..

2 recordsLinked to original sources

Novel cumate-inducible models of MYC-driven neuroblastoma enable unconfounded mitochondrial synthetic lethality screens

Oncogenic MYC transcription factors profoundly alter cellular programs, imposing dependencies that can be therapeutically exploited in MYC-driven cancers such as high-risk neuroblastoma. However, dissecting such synthetic lethal vulnerabilities using controlled, tunable gene expression within a uniform genetic background remains challenging. Widely used tetracycline-regulated systems rely on inducers known to perturb mitochondrial function, introducing significant off-target effects that may confound interpretation. To overcome this limitation, we established novel cumate (p-isopropylbenzoate)-inducible neuroblastoma models that enable physiologically unbiased regulation of MYC(N) expression. Functional validation demonstrated that cumate itself does not induce off-target effects on neuroblastoma cell viability, mitochondrial membrane potential, morphology, proteostasis, or stress signaling, even at the highest recommended dose. The developed SHEP-CuO-MYC and -MYCN models show efficient, titratable, and reversible upregulation of c-MYC and N-MYC, respectively, recapitulating the expression levels observed in MYC(N)-amplified neuroblastoma. As a proof-of-concept, we applied these models to mechanistically validate the recently proposed mitoribosomal synthetic lethality, providing fully unbiased evidence that elevated c-MYC/N-MYC levels sensitize neuroblastoma cells to inhibitors of mitochondrial gene expression. Although impairing mitochondrial translation activated mitochondrial integrated stress response in both MYC-on and MYC-off states, it led to dramatic MYC downregulation coupled with enhanced caspase-dependent cell death in MYC-on cells. These findings reveal that MYC(N) overexpression confers a selective, proliferation-independent mitochondrial vulnerability that can be therapeutically targeted by repurposing well-tolerated mitochondrial ribosome-targeting antibiotics. Collectively, our models provide a robust platform for studying the MYC-mitochondria interplay and can be directly adapted for drug repurposing screens targeting mitochondrial dependencies in neuroblastoma and, potentially, other MYC-driven tumors. HIGHLIGHTSO_LICumate shows no inducer-associated mitochondrial or cytotoxic off-target effects C_LIO_LICumate-inducible MYC models enable mechanistic studies of mitochondrial synthetic lethality C_LIO_LIMYC overexpression drives neuroblastoma sensitivity to mitochondrial translation inhibition C_LIO_LICommon ribosomal antibiotics trigger caspase-dependent cell death in MYC-driven tumor cells C_LIO_LIContext-specific MYC downregulation links mitochondrial stress to MYC synthetic lethality C_LI

cancer biology↗

Uncovering Functional Distant Mutations by Ultra-High-Throughput Screening of Dehalogenases

Conformational dynamics play a central role in enzyme function by controlling substrate access and productive binding. Yet mutations that beneficially modulate these properties are difficult to identify. Here, we used ultrahigh-throughput fluorescence-activated droplet sorting (FADS) with a bulky fluorogenic substrate derived from coumarin (COU-3) to impose steric selection pressure on the haloalkane dehalogenase LinB. Screening a focused library yielded five single substitutions located 11.5-15.5 [A] from the catalytic centre. Variant I138N showed a fourfold increase in catalytic efficiency toward COU-3 through reduced KM and increased kcat, associated with increased cap-domain flexibility and facilitated substrate entry. In contrast, variant P208S markedly reduced substrate inhibition and shifted specificity toward bulkier iodinated haloalkanes by reshaping its tunnel environment. Integrated kinetic and structural analyses revealed that screening with bulky substrates directs selection toward distal regions controlling substrate access and unproductive binding. These findings demonstrate that ultrahigh-throughput FADS can reveal dynamic mechanisms of enzyme adaptation that remain difficult to predict by rational design. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=183 SRC="FIGDIR/small/713925v1_ufig1.gif" ALT="Figure 1"> View larger version (51K): org.highwire.dtl.DTLVardef@782038org.highwire.dtl.DTLVardef@8b43f3org.highwire.dtl.DTLVardef@11a403eorg.highwire.dtl.DTLVardef@6fcaea_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗