Mtor
M. musculus
mechanistic target of rapamycin kinase
What the model saw
Gene: Mtor Organism: Mus musculus Known functions: mechanistic target of rapamycin kinase. serine/threonine-protein kinase mTOR. RNA polymerase III type 1 promoter sequence-specific DNA binding. RNA polymerase III type 2 promoter sequence-specific DNA binding. RNA polymerase III type 3 promoter sequence-specific DNA binding. TFIIIC-class transcription factor complex binding. identical protein binding. inositol hexakisphosphate binding. kinase activity. non-membrane spanning protein tyrosine kinase activity. phosphoprotein binding. protein binding. protein domain specific binding. protein kinase activity. protein kinase binding. protein serine kinase activity. protein serine/threonine kinase activity. protein tyrosine kinase activity. protein-containing complex binding. ribosome binding. transmembrane transporter binding.
View unredacted entry
mechanistic target of rapamycin kinase. serine/threonine-protein kinase mTOR. RNA polymerase III type 1 promoter sequence-specific DNA binding. RNA polymerase III type 2 promoter sequence-specific DNA binding. RNA polymerase III type 3 promoter sequence-specific DNA binding. TFIIIC-class transcription factor complex binding. identical protein binding. inositol hexakisphosphate binding. kinase activity. non-membrane spanning protein tyrosine kinase activity. phosphoprotein binding. protein binding. protein domain specific binding. protein kinase activity. protein kinase binding. protein serine kinase activity. protein serine/threonine kinase activity. protein tyrosine kinase activity. protein-containing complex binding. ribosome binding. transmembrane transporter binding.
Solver output
mTOR (mechanistic target of rapamycin) is the catalytic serine/threonine kinase subunit of mTORC1 and mTORC2 complexes, which serve as master regulators of nutrient sensing and anabolic metabolism. When active, mTORC1 phosphorylates S6K1 and 4E-BP1 to promote ribosome biogenesis, protein synthesis, and cell growth while simultaneously suppressing autophagy via ULK1 phosphorylation. Chronic mTOR hyperactivation accelerates aging phenotypes by inhibiting macroautophagy, impairing proteostasis, and driving cellular senescence. Genetic reduction of mTOR activity (e.g., hypomorphic Mtor alleles, rapamycin treatment) consistently extends lifespan in mice, Drosophila, C. elegans, and yeast, establishing mTOR's normal function as pro-growth and anti-longevity. The gene's additional annotations—ribosome binding, RNA Pol III promoter binding, and transmembrane transporter binding—further underscore its broad anabolic role that opposes longevity when constitutively active.
GenAge curators classify each gene's normal function as promoting (Pro-Longevity) or opposing (Anti-Longevity) longevity, based on synthesis across studies. Loss-of-function effects can vary from this depending on the manipulation.
Advisor judgment
The model correctly identified mTOR as anti_longevity with very high confidence (0.95). The mechanistic reasoning is excellent and accurate: mTOR as a master regulator of nutrient sensing, mTORC1 phosphorylation of S6K1 and 4E-BP1, autophagy suppression via ULK1, and the well-established finding that genetic reduction of mTOR activity extends lifespan in mice. The model also correctly notes the cross-species conservation of this effect. All key pathways cited are accurate and relevant. The reasoning is comprehensive and well-grounded in the literature.
Raw API responses
solver
{
"reasoning": "mTOR (mechanistic target of rapamycin) is the catalytic serine/threonine kinase subunit of mTORC1 and mTORC2 complexes, which serve as master regulators of nutrient sensing and anabolic metabolism. When active, mTORC1 phosphorylates S6K1 and 4E-BP1 to promote ribosome biogenesis, protein synthesis, and cell growth while simultaneously suppressing autophagy via ULK1 phosphorylation. Chronic mTOR hyperactivation accelerates aging phenotypes by inhibiting macroautophagy, impairing proteostasis, and driving cellular senescence. Genetic reduction of mTOR activity (e.g., hypomorphic Mtor alleles, rapamycin treatment) consistently extends lifespan in mice, Drosophila, C. elegans, and yeast, establishing mTOR's normal function as pro-growth and anti-longevity. The gene's additional annotations—ribosome binding, RNA Pol III promoter binding, and transmembrane transporter binding—further underscore its broad anabolic role that opposes longevity when constitutively active.",
"confidence": 0.95,
"key_pathways": [
"mTORC1/S6K1-4E-BP1 nutrient sensing axis",
"autophagy suppression via ULK1 phosphorylation",
"ribosome biogenesis and protein synthesis"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly identified mTOR as anti_longevity with very high confidence (0.95). The mechanistic reasoning is excellent and accurate: mTOR as a master regulator of nutrient sensing, mTORC1 phosphorylation of S6K1 and 4E-BP1, autophagy suppression via ULK1, and the well-established finding that genetic reduction of mTOR activity extends lifespan in mice. The model also correctly notes the cross-species conservation of this effect. All key pathways cited are accurate and relevant. The reasoning is comprehensive and well-grounded in the literature.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}