ifg-1
C. elegans
MIF4G domain-containing protein
What the model saw
Gene: ifg-1 Organism: Caenorhabditis elegans Known functions: MIF4G domain-containing protein. RNA binding. mRNA binding. translation initiation factor activity.
View unredacted entry
MIF4G domain-containing protein. RNA binding. mRNA binding. translation initiation factor activity.
Solver output
ifg-1 encodes the C. elegans ortholog of eIF4G, a central scaffold protein of the eIF4F translation initiation complex. As a translation initiation factor with MIF4G domain and mRNA-binding activity, ifg-1 promotes cap-dependent mRNA translation, which is a major downstream effector of the TOR (Target of Rapamycin) nutrient-sensing pathway. Elevated TOR signaling upregulates eIF4F complex activity to drive global protein synthesis, and this is a well-established pro-aging axis in C. elegans. Reduction of ifg-1 function has been shown to extend lifespan in C. elegans, consistent with the broader paradigm that dampening cap-dependent translation (e.g., via TOR inhibition or reduced eIF4G activity) promotes longevity by reducing anabolic load and potentially enhancing stress resistance and proteostasis. Thus, the normal pro-translational function of ifg-1 opposes 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 ifg-1. The mechanistic reasoning is accurate and well-detailed: ifg-1 encodes the C. elegans eIF4G ortholog, a key scaffold in the eIF4F translation initiation complex downstream of TOR signaling. Reduction of ifg-1 extends lifespan in C. elegans, making it anti-longevity in its normal function. The model correctly identified the TOR/cap-dependent translation axis, eIF4F complex assembly, and the proteostasis/anabolic load rationale. High confidence (0.82) is appropriate given the well-established literature on this gene.
Raw API responses
solver
{
"reasoning": "ifg-1 encodes the C. elegans ortholog of eIF4G, a central scaffold protein of the eIF4F translation initiation complex. As a translation initiation factor with MIF4G domain and mRNA-binding activity, ifg-1 promotes cap-dependent mRNA translation, which is a major downstream effector of the TOR (Target of Rapamycin) nutrient-sensing pathway. Elevated TOR signaling upregulates eIF4F complex activity to drive global protein synthesis, and this is a well-established pro-aging axis in C. elegans. Reduction of ifg-1 function has been shown to extend lifespan in C. elegans, consistent with the broader paradigm that dampening cap-dependent translation (e.g., via TOR inhibition or reduced eIF4G activity) promotes longevity by reducing anabolic load and potentially enhancing stress resistance and proteostasis. Thus, the normal pro-translational function of ifg-1 opposes longevity.",
"confidence": 0.82,
"key_pathways": [
"TOR signaling / cap-dependent translation initiation",
"eIF4F complex assembly",
"mRNA translation regulation"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for ifg-1. The mechanistic reasoning is accurate and well-detailed: ifg-1 encodes the C. elegans eIF4G ortholog, a key scaffold in the eIF4F translation initiation complex downstream of TOR signaling. Reduction of ifg-1 extends lifespan in C. elegans, making it anti-longevity in its normal function. The model correctly identified the TOR/cap-dependent translation axis, eIF4F complex assembly, and the proteostasis/anabolic load rationale. High confidence (0.82) is appropriate given the well-established literature on this gene.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}