gpc-1
C. elegans
Guanine nucleotide-binding protein subunit gamma
What the model saw
Gene: gpc-1 Organism: Caenorhabditis elegans Known functions: Guanine nucleotide-binding protein subunit gamma. G-protein beta-subunit binding.
View unredacted entry
Guanine nucleotide-binding protein subunit gamma. G-protein beta-subunit binding.
Solver output
gpc-1 encodes a Gγ (G-protein gamma) subunit that obligatorily heterodimerizes with a Gβ subunit to form the Gβγ complex, which modulates the activity of Gα subunits in heterotrimeric G-protein signaling. In C. elegans, Gβγ signaling (particularly through GOA-1/Gαo and EGL-30/Gαq pathways) is known to antagonize longevity-promoting pathways. The Gβγ dimer can activate downstream effectors that promote insulin/IGF-1-like signaling or inhibit DAF-16/FOXO nuclear activity, thereby reducing lifespan. Loss-of-function in Gγ subunits in C. elegans has been associated with extended lifespan, consistent with the normal function of gpc-1 being anti-longevity. This places gpc-1's primary mechanism within deregulated nutrient sensing, as G-protein signaling in C. elegans is tightly coupled to the insulin/IGF-1 and neuroendocrine nutrient-sensing axes.
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 gpc-1. The mechanistic reasoning is plausible and well-structured - gpc-1 encodes a Gγ subunit that forms the Gβγ complex, and the model correctly identifies that loss-of-function in Gγ subunits extends lifespan, making the normal function anti-longevity. The connection to insulin/IGF-1 signaling and DAF-16/FOXO is reasonable, though the specific mechanistic link between Gβγ and nutrient sensing could be more directly supported. The confidence level of 0.62 is appropriately moderate given the indirect evidence. Overall, solid reasoning with a correct answer.
Raw API responses
solver
{
"reasoning": "gpc-1 encodes a Gγ (G-protein gamma) subunit that obligatorily heterodimerizes with a Gβ subunit to form the Gβγ complex, which modulates the activity of Gα subunits in heterotrimeric G-protein signaling. In C. elegans, Gβγ signaling (particularly through GOA-1/Gαo and EGL-30/Gαq pathways) is known to antagonize longevity-promoting pathways. The Gβγ dimer can activate downstream effectors that promote insulin/IGF-1-like signaling or inhibit DAF-16/FOXO nuclear activity, thereby reducing lifespan. Loss-of-function in Gγ subunits in C. elegans has been associated with extended lifespan, consistent with the normal function of gpc-1 being anti-longevity. This places gpc-1's primary mechanism within deregulated nutrient sensing, as G-protein signaling in C. elegans is tightly coupled to the insulin/IGF-1 and neuroendocrine nutrient-sensing axes.",
"confidence": 0.62,
"key_pathways": [
"Heterotrimeric G-protein signaling (Gβγ complex)",
"Insulin/IGF-1 signaling pathway (DAF-2/DAF-16 axis)",
"Gαo/Gαq neuroendocrine signaling"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for gpc-1. The mechanistic reasoning is plausible and well-structured - gpc-1 encodes a Gγ subunit that forms the Gβγ complex, and the model correctly identifies that loss-of-function in Gγ subunits extends lifespan, making the normal function anti-longevity. The connection to insulin/IGF-1 signaling and DAF-16/FOXO is reasonable, though the specific mechanistic link between Gβγ and nutrient sensing could be more directly supported. The confidence level of 0.62 is appropriately moderate given the indirect evidence. Overall, solid reasoning with a correct answer.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}