ragc-1
C. elegans
Ras-related GTP-binding protein C
What the model saw
Gene: ragc-1 Organism: Caenorhabditis elegans Known functions: Ras-related GTP-binding protein C. GTP binding. GTPase activity.
View unredacted entry
Ras-related GTP-binding protein C. GTP binding. GTPase activity.
Solver output
RAGC-1 is the C. elegans ortholog of mammalian RagC (RRAGC), a Ras-family GTPase that forms obligate heterodimers with RagA/B (RAGA-1 in C. elegans) to recruit mTORC1 to the lysosomal surface in response to amino acid availability. In the active signaling state, RagC/D is GDP-loaded while RagA/B is GTP-loaded, enabling mTORC1 activation. By facilitating mTORC1 complex recruitment and activation, RAGC-1 promotes nutrient-sensing signaling that suppresses autophagy and drives anabolic processes. Downregulation of TORC1 signaling — including loss-of-function in Rag GTPase components — is well established to extend lifespan in C. elegans and other model organisms by mimicking dietary restriction and promoting autophagy. Therefore, the normal pro-mTORC1 function of RAGC-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 ragc-1 in C. elegans. The mechanistic reasoning is excellent and accurate: RAGC-1 is the RagC ortholog that forms heterodimers with RAGA-1 to recruit mTORC1 to the lysosomal surface in response to amino acids. The model correctly explains that loss-of-function in Rag GTPase components reduces TORC1 signaling, mimicking dietary restriction and extending lifespan. The explanation of RagC being GDP-loaded in the active state while RagA/B is GTP-loaded is biochemically accurate. The confidence level of 0.82 is appropriate given the well-established role of TOR signaling in longevity.
Raw API responses
solver
{
"reasoning": "RAGC-1 is the C. elegans ortholog of mammalian RagC (RRAGC), a Ras-family GTPase that forms obligate heterodimers with RagA/B (RAGA-1 in C. elegans) to recruit mTORC1 to the lysosomal surface in response to amino acid availability. In the active signaling state, RagC/D is GDP-loaded while RagA/B is GTP-loaded, enabling mTORC1 activation. By facilitating mTORC1 complex recruitment and activation, RAGC-1 promotes nutrient-sensing signaling that suppresses autophagy and drives anabolic processes. Downregulation of TORC1 signaling — including loss-of-function in Rag GTPase components — is well established to extend lifespan in C. elegans and other model organisms by mimicking dietary restriction and promoting autophagy. Therefore, the normal pro-mTORC1 function of RAGC-1 opposes longevity.",
"confidence": 0.82,
"key_pathways": [
"mTORC1 lysosomal recruitment via Rag GTPase heterodimer",
"amino acid sensing / TOR nutrient signaling",
"autophagy suppression downstream of TORC1"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for ragc-1 in C. elegans. The mechanistic reasoning is excellent and accurate: RAGC-1 is the RagC ortholog that forms heterodimers with RAGA-1 to recruit mTORC1 to the lysosomal surface in response to amino acids. The model correctly explains that loss-of-function in Rag GTPase components reduces TORC1 signaling, mimicking dietary restriction and extending lifespan. The explanation of RagC being GDP-loaded in the active state while RagA/B is GTP-loaded is biochemically accurate. The confidence level of 0.82 is appropriate given the well-established role of TOR signaling in longevity.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}