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Panto, C.

Publications and source records attributed to Panto, C..

2 recordsLinked to original sources

Pre-symptomatic proteomic and metabolomic profiling identifies compensated ER-redox-metabolic adaptation and early nuclear vulnerability in neuronal ERO1L toxicity

Aging progressively challenges neuronal proteostasis, redox homeostasis, and metabolism, yet the molecular changes that precede functional decline remain poorly understood. Endoplasmic reticulum oxidoreductin 1 (ERO1), a key regulator of oxidative protein folding, links endoplasmic reticulum (ER) proteostasis with cellular redox balance and is elevated in aging and neurodegenerative contexts. Here, we investigated how neuronal ERO1L elevation reshapes cellular homeostasis before overt dysfunction in Drosophila melanogaster. Endogenous ERO1L expression increased with age, and neuronal ERO1L elevation shortened lifespan and caused progressive locomotor decline. This effect was strongly cell-type dependent, as ERO1L elevation in glia, muscle, or fat body did not produce a comparable survival phenotype. At day 5 post-eclosion, locomotor performance remained preserved and major brain reactive-oxygen-species (ROS) accumulation was not yet detectable, defining a pre-symptomatic stage. Multi-omic profiling at this stage revealed selective remodelling of ER proteostasis, redox defence, and mitochondrial-energy pathways, together with changes in central-carbon, nitrogen, and purine metabolism. In contrast to these broadly adaptive responses, chromatin- and RNA-homeostasis-associated proteins were selectively reduced, accompanied by decreased HP1, dFmr1, and Piwi expression and increased transposable-element transcripts. Thus, neuronal ERO1L elevation establishes a pre-symptomatic state in which proteostatic and metabolic adaptation coexists with early vulnerability of nuclear and RNA-homeostasis pathways, preceding overt oxidative stress and behavioural decline. These findings provide an in vivo framework to investigate how age-associated ERO1L elevation may progressively reduce neuronal resilience during brain aging.

neuroscience↗

A leukemia-derived ENL/AF9 chemical probe enhances neuronal stress resilience and ameliorates ALS phenotypes

Chemical perturbation of chromatin reader proteins provides a precise strategy to interrogate epigenetic control of neuronal stress adaptation. ENL and AF9 are YEATS-domain acyl-lysine readers best characterized in leukemia, but their roles in neurons remain unclear. Here, we use the selective YEATS inhibitor SR-0813 to define ENL/AF9 function in neuronal stress responses across Drosophila and human systems. SR-0813 phenocopies genetic ENL/AF9 reduction by extending lifespan and enhancing stress tolerance in vivo, and improves survival of human neurons under multiple stress conditions, with the strongest effects during endoplasmic reticulum stress. Mechanistically, SR-0813 attenuates PERK-ISR signaling and reduces apoptotic commitment without broadly enhancing proteostasis capacity. Notably, its effects are highly context dependent, conferring protection in stress-signaling-driven models but reduced efficacy or detrimental outcomes under chronic aggregation or mitochondrial stress. These findings identify ENL/AF9 as modulators of stress-response dynamics and highlight YEATS-domain inhibition as a context-dependent strategy to reshape neuronal resilience. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=181 HEIGHT=200 SRC="FIGDIR/small/717610v2_ufig1.gif" ALT="Figure 1"> View larger version (46K): org.highwire.dtl.DTLVardef@e7bee4org.highwire.dtl.DTLVardef@a59d76org.highwire.dtl.DTLVardef@104dd7eorg.highwire.dtl.DTLVardef@69bb51_HPS_FORMAT_FIGEXP M_FIG C_FIG siRNA or the YEATS-domain inhibitor SR-0813 suppress the acyl-lysine reader ENL/AF9, extending lifespan and increasing H2O2 tolerance in Drosophila. In neurons (Drosophila and SH-SY5Y), ENL/AF9 inhibition lowers PERK-ISR signaling and apoptosis while maintaining proteostasis. Effects are context dependent: protective under UPR/ISR-dominant stress but potentially detrimental under aggregation or mitochondrial stress. Created with BioRender.

cell biology↗