Pten
M. musculus
phosphatase and tensin homolog
What the model saw
Gene: Pten Organism: Mus musculus Known functions: phosphatase and tensin homolog. phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN. PDZ domain binding. anaphase-promoting complex binding. beta-catenin binding. enzyme binding. identical protein binding. inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity. inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity. ionotropic glutamate receptor binding. molecular function inhibitor activity. phosphatase activity. phosphatidylinositol phosphate phosphatase activity. phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity. phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity. phosphatidylinositol-3-phosphate phosphatase activity. phosphoprotein phosphatase activity. platelet-derived growth factor receptor binding. protein binding. protein kinase binding. protein serine/threonine phosphatase activity. protein tyrosine kinase binding. protein tyrosine phosphatase activity. ubiquitin ligase activator activity. ubiquitin-specific protease binding.
View unredacted entry
phosphatase and tensin homolog. phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN. PDZ domain binding. anaphase-promoting complex binding. beta-catenin binding. enzyme binding. identical protein binding. inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity. inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity. ionotropic glutamate receptor binding. molecular function inhibitor activity. phosphatase activity. phosphatidylinositol phosphate phosphatase activity. phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity. phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity. phosphatidylinositol-3-phosphate phosphatase activity. phosphoprotein phosphatase activity. platelet-derived growth factor receptor binding. protein binding. protein kinase binding. protein serine/threonine phosphatase activity. protein tyrosine kinase binding. protein tyrosine phosphatase activity. ubiquitin ligase activator activity. ubiquitin-specific protease binding.
Solver output
PTEN is a phosphatidylinositol-3,4,5-trisphosphate (PIP3) 3-phosphatase that directly antagonizes PI3K signaling by dephosphorylating PIP3 to PIP2, thereby suppressing AKT/mTOR activation. Reduced PI3K-AKT-mTOR signaling is one of the most conserved pro-longevity interventions across model organisms, including mice. By restraining this nutrient-sensing axis, PTEN promotes cellular quiescence, reduces anabolic metabolism, and enhances stress resistance. Additionally, PTEN's tumor-suppressive role limits oncogenic transformation, reducing cancer-related mortality. Mouse models with elevated PTEN expression show extended lifespan, while loss of PTEN leads to hyperactivated mTORC1 and accelerated aging phenotypes.
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 predicted PTEN as pro_longevity with high confidence (0.92). The mechanistic reasoning is excellent and accurate: PTEN dephosphorylates PIP3 to PIP2, antagonizing PI3K-AKT-mTOR signaling, which is a well-established pro-longevity pathway. The model correctly notes that mouse models with elevated PTEN expression show extended lifespan (referencing the Alimonti et al. 2012 and Ortega-Molina et al. 2012 studies showing super-PTEN mice live longer). The tumor suppression angle is also correctly identified as contributing to longevity. The mechanism classification as "deregulated_nutrient_sensing" is appropriate. All aspects of the prediction are accurate and well-reasoned.
Raw API responses
solver
{
"reasoning": "PTEN is a phosphatidylinositol-3,4,5-trisphosphate (PIP3) 3-phosphatase that directly antagonizes PI3K signaling by dephosphorylating PIP3 to PIP2, thereby suppressing AKT/mTOR activation. Reduced PI3K-AKT-mTOR signaling is one of the most conserved pro-longevity interventions across model organisms, including mice. By restraining this nutrient-sensing axis, PTEN promotes cellular quiescence, reduces anabolic metabolism, and enhances stress resistance. Additionally, PTEN's tumor-suppressive role limits oncogenic transformation, reducing cancer-related mortality. Mouse models with elevated PTEN expression show extended lifespan, while loss of PTEN leads to hyperactivated mTORC1 and accelerated aging phenotypes.",
"confidence": 0.92,
"key_pathways": [
"PI3K-AKT-mTOR nutrient sensing axis",
"Insulin/IGF-1 signaling pathway",
"Tumor suppression via PIP3 dephosphorylation"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted PTEN as pro_longevity with high confidence (0.92). The mechanistic reasoning is excellent and accurate: PTEN dephosphorylates PIP3 to PIP2, antagonizing PI3K-AKT-mTOR signaling, which is a well-established pro-longevity pathway. The model correctly notes that mouse models with elevated PTEN expression show extended lifespan (referencing the Alimonti et al. 2012 and Ortega-Molina et al. 2012 studies showing super-PTEN mice live longer). The tumor suppression angle is also correctly identified as contributing to longevity. The mechanism classification as \"deregulated_nutrient_sensing\" is appropriate. All aspects of the prediction are accurate and well-reasoned.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}