ced-3
C. elegans
Cell death protein 3 subunit p17
What the model saw
Gene: ced-3 Organism: Caenorhabditis elegans Known functions: Cell [REDACTED] protein 3 subunit p17. cysteine-type endopeptidase activator activity. cysteine-type endopeptidase activator activity involved in apoptotic process. cysteine-type endopeptidase activity. cysteine-type peptidase activity. endopeptidase activity. enzyme activator activity. identical protein binding. protein binding.
View unredacted entry
Cell death protein 3 subunit p17. cysteine-type endopeptidase activator activity. cysteine-type endopeptidase activator activity involved in apoptotic process. cysteine-type endopeptidase activity. cysteine-type peptidase activity. endopeptidase activity. enzyme activator activity. identical protein binding. protein binding.
Solver output
CED-3 is the founding member of the caspase family in C. elegans and functions as the primary executioner cysteine-type endopeptidase in the apoptotic cascade. Its activation drives programmed cell death, and while developmental apoptosis is essential, excessive or dysregulated CED-3 activity promotes organismal aging by eliminating cells — including stem-like and somatic cells — that could otherwise contribute to tissue maintenance and repair. Loss-of-function mutations in ced-3 have been associated with extended lifespan in C. elegans, consistent with reduced apoptotic cell loss preserving tissue homeostasis. CED-3 acts downstream of CED-4 (Apaf-1 homolog) and upstream of cellular dismantling, placing it at the effector step of the apoptotic program. Its role as both an endopeptidase and an activator of other caspase-like activities amplifies pro-death signaling, making its normal function antagonistic to 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 identifies CED-3 as anti_longevity with high confidence (0.82). The mechanistic reasoning is largely correct: CED-3 is the primary executioner caspase in C. elegans apoptosis, and its loss-of-function extends lifespan. The model correctly places it in the CED-3/CED-4/CED-9 pathway and explains why it is anti-longevity (promotes cell death, reducing tissue maintenance capacity). The mechanism_class of "cellular_senescence" is slightly off — CED-3 is more accurately classified under apoptosis/programmed cell death rather than cellular senescence, which is a distinct process. However, the overall mechanistic narrative about apoptosis driving aging is sound. The claim that "loss-of-function mutations in ced-3 have been associated with extended lifespan" is the key correct mechanistic point. Minor issue: the model labels the mechanism as "cellular_senescence" which is technically incorrect (should be apoptosis), but the textual reasoning correctly describes apoptosis throughout.
Raw API responses
solver
{
"reasoning": "CED-3 is the founding member of the caspase family in C. elegans and functions as the primary executioner cysteine-type endopeptidase in the apoptotic cascade. Its activation drives programmed cell death, and while developmental apoptosis is essential, excessive or dysregulated CED-3 activity promotes organismal aging by eliminating cells — including stem-like and somatic cells — that could otherwise contribute to tissue maintenance and repair. Loss-of-function mutations in ced-3 have been associated with extended lifespan in C. elegans, consistent with reduced apoptotic cell loss preserving tissue homeostasis. CED-3 acts downstream of CED-4 (Apaf-1 homolog) and upstream of cellular dismantling, placing it at the effector step of the apoptotic program. Its role as both an endopeptidase and an activator of other caspase-like activities amplifies pro-death signaling, making its normal function antagonistic to longevity.",
"confidence": 0.82,
"key_pathways": [
"CED-3/CED-4/CED-9 apoptosis pathway",
"caspase-mediated programmed cell death",
"tissue homeostasis via apoptotic regulation"
],
"mechanism_class": "cellular_senescence",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly identifies CED-3 as anti_longevity with high confidence (0.82). The mechanistic reasoning is largely correct: CED-3 is the primary executioner caspase in C. elegans apoptosis, and its loss-of-function extends lifespan. The model correctly places it in the CED-3/CED-4/CED-9 pathway and explains why it is anti-longevity (promotes cell death, reducing tissue maintenance capacity). The mechanism_class of \"cellular_senescence\" is slightly off — CED-3 is more accurately classified under apoptosis/programmed cell death rather than cellular senescence, which is a distinct process. However, the overall mechanistic narrative about apoptosis driving aging is sound. The claim that \"loss-of-function mutations in ced-3 have been associated with extended lifespan\" is the key correct mechanistic point. Minor issue: the model labels the mechanism as \"cellular_senescence\" which is technically incorrect (should be apoptosis), but the textual reasoning correctly describes apoptosis throughout.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}