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Ilp2

D. melanogaster

Insulin-like peptide 2

What the model saw

Gene: Ilp2
Organism: Drosophila melanogaster
Known functions: Insulin-like peptide 2. hormone activity. insulin receptor binding. receptor ligand activity.
View unredacted entry
Insulin-like peptide 2. hormone activity. insulin receptor binding. receptor ligand activity.

Solver output

Predicted influence
Anti-longevity
Confidence
93%
Mechanism
Deregulated nutrient sensing
Reasoning

Ilp2 (Insulin-like peptide 2) is a secreted ligand that binds and activates the Drosophila insulin receptor (dInR), directly stimulating the insulin/IGF-1 signaling (IIS) pathway. Activation of IIS promotes phosphorylation of Akt/PKB, which inhibits the FOXO transcription factor dFOXO by retaining it in the cytoplasm. Reduced IIS — achieved by loss-of-function of insulin-like peptides or their receptor — is one of the most robust pro-longevity interventions in Drosophila, extending lifespan substantially. Conversely, normal (or elevated) Ilp2 activity drives anabolic growth and suppresses stress-resistance and autophagy programs downstream of dFOXO. Therefore, the normal function of Ilp2 as an activating ligand of the IIS pathway opposes longevity.

Key pathways
Insulin/IGF-1 signaling (IIS)dFOXO transcription factor regulationPI3K/Akt signaling
Longevity influence
Anti-longevity
Lifespan effect
Increase

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

Answer
Correct
Mechanism
Correct
Reasoning quality
5/5
Failure mode
Correct
Notes

The model correctly predicted anti_longevity for Ilp2 with high confidence (0.93). The mechanistic reasoning is thorough and accurate: Ilp2 activates the insulin/IGF-1 signaling pathway via the Drosophila insulin receptor, which inhibits dFOXO through Akt/PKB phosphorylation, suppressing stress resistance and autophagy programs. The well-established finding that reduced IIS extends lifespan in Drosophila is correctly cited, and the conclusion that Ilp2 as an activating ligand opposes longevity is sound. Key pathways identified (IIS, dFOXO, PI3K/Akt) are all relevant and correct.

Raw API responses

solver

{
  "reasoning": "Ilp2 (Insulin-like peptide 2) is a secreted ligand that binds and activates the Drosophila insulin receptor (dInR), directly stimulating the insulin/IGF-1 signaling (IIS) pathway. Activation of IIS promotes phosphorylation of Akt/PKB, which inhibits the FOXO transcription factor dFOXO by retaining it in the cytoplasm. Reduced IIS — achieved by loss-of-function of insulin-like peptides or their receptor — is one of the most robust pro-longevity interventions in Drosophila, extending lifespan substantially. Conversely, normal (or elevated) Ilp2 activity drives anabolic growth and suppresses stress-resistance and autophagy programs downstream of dFOXO. Therefore, the normal function of Ilp2 as an activating ligand of the IIS pathway opposes longevity.",
  "confidence": 0.93,
  "key_pathways": [
    "Insulin/IGF-1 signaling (IIS)",
    "dFOXO transcription factor regulation",
    "PI3K/Akt signaling"
  ],
  "mechanism_class": "deregulated_nutrient_sensing",
  "longevity_influence": "anti_longevity"
}

advisor

{
  "notes": "The model correctly predicted anti_longevity for Ilp2 with high confidence (0.93). The mechanistic reasoning is thorough and accurate: Ilp2 activates the insulin/IGF-1 signaling pathway via the Drosophila insulin receptor, which inhibits dFOXO through Akt/PKB phosphorylation, suppressing stress resistance and autophagy programs. The well-established finding that reduced IIS extends lifespan in Drosophila is correctly cited, and the conclusion that Ilp2 as an activating ligand opposes longevity is sound. Key pathways identified (IIS, dFOXO, PI3K/Akt) are all relevant and correct.",
  "failure_mode": "correct",
  "answer_correct": true,
  "mechanism_correct": true,
  "reasoning_quality": 5,
  "ground_truth_questionable": false
}