AGP1
S. cerevisiae
amino acid transporter AGP1
What the model saw
Gene: AGP1 Organism: Saccharomyces cerevisiae Known functions: amino acid transporter AGP1. L-phenylalanine transmembrane transporter activity. L-proline transmembrane transporter activity. amino acid transmembrane transporter activity.
View unredacted entry
amino acid transporter AGP1. L-phenylalanine transmembrane transporter activity. L-proline transmembrane transporter activity. amino acid transmembrane transporter activity.
Solver output
AGP1 encodes a broad-specificity amino acid permease in S. cerevisiae that facilitates uptake of multiple amino acids including L-phenylalanine and L-proline across the plasma membrane. Increased intracellular amino acid availability, particularly of branched-chain and aromatic amino acids, is a well-established activator of the TORC1 (Target of Rapamycin Complex 1) nutrient-sensing pathway. Elevated TORC1 signaling suppresses autophagy and stress-response programs that are pro-longevity, and dietary restriction-mediated lifespan extension in yeast is partly achieved by reducing amino acid import and TORC1 activity. Thus, AGP1's normal function of importing amino acids promotes TORC1 activation, which is anti-longevity. Consistent with this, deletion of amino acid permeases in yeast has been associated with lifespan extension phenotypes linked to reduced nutrient signaling.
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 AGP1 as anti_longevity. The mechanistic reasoning is sound and well-articulated: AGP1 imports amino acids, which activates TORC1 signaling, suppressing autophagy and stress responses that promote longevity. The connection between amino acid permease activity and TORC1-mediated lifespan shortening is a well-established pathway in yeast aging research. The model appropriately noted that deletion of amino acid permeases is associated with lifespan extension. Confidence of 0.62 is reasonable given the indirect nature of the evidence. The reasoning is coherent and biologically plausible, though it relies somewhat on general principles rather than AGP1-specific experimental data.
Raw API responses
solver
{
"reasoning": "AGP1 encodes a broad-specificity amino acid permease in S. cerevisiae that facilitates uptake of multiple amino acids including L-phenylalanine and L-proline across the plasma membrane. Increased intracellular amino acid availability, particularly of branched-chain and aromatic amino acids, is a well-established activator of the TORC1 (Target of Rapamycin Complex 1) nutrient-sensing pathway. Elevated TORC1 signaling suppresses autophagy and stress-response programs that are pro-longevity, and dietary restriction-mediated lifespan extension in yeast is partly achieved by reducing amino acid import and TORC1 activity. Thus, AGP1's normal function of importing amino acids promotes TORC1 activation, which is anti-longevity. Consistent with this, deletion of amino acid permeases in yeast has been associated with lifespan extension phenotypes linked to reduced nutrient signaling.",
"confidence": 0.62,
"key_pathways": [
"TORC1 nutrient sensing",
"amino acid import / plasma membrane transport",
"autophagy suppression via TOR"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted AGP1 as anti_longevity. The mechanistic reasoning is sound and well-articulated: AGP1 imports amino acids, which activates TORC1 signaling, suppressing autophagy and stress responses that promote longevity. The connection between amino acid permease activity and TORC1-mediated lifespan shortening is a well-established pathway in yeast aging research. The model appropriately noted that deletion of amino acid permeases is associated with lifespan extension. Confidence of 0.62 is reasonable given the indirect nature of the evidence. The reasoning is coherent and biologically plausible, though it relies somewhat on general principles rather than AGP1-specific experimental data.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}