myo
D. melanogaster
myoglianin
What the model saw
Gene: myo Organism: Drosophila melanogaster Known functions: myoglianin. activin receptor binding. cytokine activity. growth factor activity. receptor ligand activity.
View unredacted entry
myoglianin. activin receptor binding. cytokine activity. growth factor activity. receptor ligand activity.
Solver output
Myoglianin (myo) is a TGF-β/myostatin-family ligand in Drosophila that binds activin receptors and acts as a negative regulator of growth and muscle mass. By signaling through the Activin/TGF-β branch (via Baboon/dSmad2), myoglianin suppresses anabolic growth programs, analogous to how myostatin restrains muscle hypertrophy in vertebrates. Restraint of growth factor signaling and nutrient-sensing pathways (including crosstalk with insulin/IGF and TOR signaling) is a well-established pro-longevity mechanism in model organisms. Reduced TOR/insulin signaling and growth rate are consistently associated with lifespan extension in Drosophila, and myoglianin's role as a negative regulator of these anabolic pathways places it in a pro-longevity context. Additionally, myoglianin has been shown to regulate autophagy and proteostasis in muscle, further supporting a pro-longevity function.
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 pro_longevity for myo (myoglianin) in Drosophila. The mechanistic reasoning is largely sound: myoglianin is indeed a TGF-β/myostatin-family ligand that signals through activin receptors and acts as a negative regulator of growth. The connection to TGF-β/Activin signaling via Baboon/dSmad2 is accurate. However, the mechanism_class of "deregulated_nutrient_sensing" is somewhat imprecise — myoglianin's primary mechanism is TGF-β/Activin signaling rather than nutrient sensing per se, though the model does acknowledge the crosstalk with insulin/IGF-TOR pathways. The claim about autophagy regulation in muscle is plausible but less well-established. Overall, the reasoning is well-constructed and the answer is correct with appropriate confidence (0.65).
Raw API responses
solver
{
"reasoning": "Myoglianin (myo) is a TGF-β/myostatin-family ligand in Drosophila that binds activin receptors and acts as a negative regulator of growth and muscle mass. By signaling through the Activin/TGF-β branch (via Baboon/dSmad2), myoglianin suppresses anabolic growth programs, analogous to how myostatin restrains muscle hypertrophy in vertebrates. Restraint of growth factor signaling and nutrient-sensing pathways (including crosstalk with insulin/IGF and TOR signaling) is a well-established pro-longevity mechanism in model organisms. Reduced TOR/insulin signaling and growth rate are consistently associated with lifespan extension in Drosophila, and myoglianin's role as a negative regulator of these anabolic pathways places it in a pro-longevity context. Additionally, myoglianin has been shown to regulate autophagy and proteostasis in muscle, further supporting a pro-longevity function.",
"confidence": 0.65,
"key_pathways": [
"TGF-β/Activin signaling (Baboon/dSmad2 axis)",
"Insulin/IGF-TOR nutrient sensing",
"Muscle growth and autophagy regulation"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted pro_longevity for myo (myoglianin) in Drosophila. The mechanistic reasoning is largely sound: myoglianin is indeed a TGF-β/myostatin-family ligand that signals through activin receptors and acts as a negative regulator of growth. The connection to TGF-β/Activin signaling via Baboon/dSmad2 is accurate. However, the mechanism_class of \"deregulated_nutrient_sensing\" is somewhat imprecise — myoglianin's primary mechanism is TGF-β/Activin signaling rather than nutrient sensing per se, though the model does acknowledge the crosstalk with insulin/IGF-TOR pathways. The claim about autophagy regulation in muscle is plausible but less well-established. Overall, the reasoning is well-constructed and the answer is correct with appropriate confidence (0.65).",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}