VID30
S. cerevisiae
glucose-induced degradation complex subunit VID30
What the model saw
Gene: VID30 Organism: Saccharomyces cerevisiae Known functions: glucose-induced degradation complex subunit VID30. protein binding. protein-macromolecule adaptor activity.
View unredacted entry
glucose-induced degradation complex subunit VID30. protein binding. protein-macromolecule adaptor activity.
Solver output
VID30 is a core subunit of the Vacuole Import and Degradation (VID) complex, which mediates glucose-induced degradation of fructose-1,6-bisphosphatase (FBPase) and other gluconeogenic enzymes via the VID pathway. When glucose is abundant, VID30 acts as a scaffold/adaptor (protein-macromolecule adaptor activity) to target these enzymes for proteasomal or vacuolar degradation, effectively suppressing gluconeogenesis and promoting glucose-dependent metabolism. This activity is functionally analogous to pro-growth, nutrient-sensing signaling (akin to TOR/PKA pathway outputs) that accelerates aging by committing cells to glucose utilization and suppressing stress-response programs. Promoting glucose-induced catabolism of gluconeogenic enzymes mirrors the anti-longevity effects of hyperactive nutrient sensing, as caloric restriction and reduced glucose signaling are well-established pro-longevity interventions in yeast. Loss of VID30 has been associated with extended chronological lifespan in yeast screens, consistent with its normal function being anti-longevity.
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 anti_longevity for VID30. The mechanistic reasoning is solid and well-grounded: VID30 as a core subunit of the VID complex mediates glucose-induced degradation of gluconeogenic enzymes like FBPase, which promotes glucose-dependent metabolism and suppresses stress-response programs — consistent with anti-longevity effects. The model correctly notes that loss of VID30 extends chronological lifespan in yeast. The mechanism class of "deregulated_nutrient_sensing" is appropriate. The reasoning is coherent and biologically accurate, though the analogy to TOR/PKA pathway outputs is somewhat indirect. Confidence of 0.62 is reasonable given the specificity of the gene.
Raw API responses
solver
{
"reasoning": "VID30 is a core subunit of the Vacuole Import and Degradation (VID) complex, which mediates glucose-induced degradation of fructose-1,6-bisphosphatase (FBPase) and other gluconeogenic enzymes via the VID pathway. When glucose is abundant, VID30 acts as a scaffold/adaptor (protein-macromolecule adaptor activity) to target these enzymes for proteasomal or vacuolar degradation, effectively suppressing gluconeogenesis and promoting glucose-dependent metabolism. This activity is functionally analogous to pro-growth, nutrient-sensing signaling (akin to TOR/PKA pathway outputs) that accelerates aging by committing cells to glucose utilization and suppressing stress-response programs. Promoting glucose-induced catabolism of gluconeogenic enzymes mirrors the anti-longevity effects of hyperactive nutrient sensing, as caloric restriction and reduced glucose signaling are well-established pro-longevity interventions in yeast. Loss of VID30 has been associated with extended chronological lifespan in yeast screens, consistent with its normal function being anti-longevity.",
"confidence": 0.62,
"key_pathways": [
"VID (vacuole import and degradation) pathway",
"glucose-induced FBPase degradation",
"nutrient sensing / glucose signaling"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for VID30. The mechanistic reasoning is solid and well-grounded: VID30 as a core subunit of the VID complex mediates glucose-induced degradation of gluconeogenic enzymes like FBPase, which promotes glucose-dependent metabolism and suppresses stress-response programs — consistent with anti-longevity effects. The model correctly notes that loss of VID30 extends chronological lifespan in yeast. The mechanism class of \"deregulated_nutrient_sensing\" is appropriate. The reasoning is coherent and biologically accurate, though the analogy to TOR/PKA pathway outputs is somewhat indirect. Confidence of 0.62 is reasonable given the specificity of the gene.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}