cct-4
C. elegans
T-complex protein 1 subunit delta
What the model saw
Gene: cct-4 Organism: Caenorhabditis elegans Known functions: T-complex protein 1 subunit delta. ATP binding. ATP hydrolysis activity. ATP-dependent protein folding chaperone. unfolded protein binding.
View unredacted entry
T-complex protein 1 subunit delta. ATP binding. ATP hydrolysis activity. ATP-dependent protein folding chaperone. unfolded protein binding.
Solver output
CCT-4 is the delta subunit of the TRiC/CCT chaperonin complex, which uses ATP hydrolysis to fold nascent and misfolded proteins into their native conformations. Proper proteostasis is a well-established determinant of longevity in C. elegans, and TRiC/CCT activity directly prevents the accumulation of misfolded and aggregated proteins that drive aging pathology. The complex is known to assist folding of cytoskeletal proteins (actin, tubulin) and other essential substrates, and its activity intersects with the broader HSP90/HSP70 chaperone network that supports stress resistance and lifespan. Loss of CCT subunit function in C. elegans leads to proteotoxic stress and reduced fitness, while maintenance of chaperonin capacity supports healthy aging by counteracting protein aggregation, a hallmark of age-related decline.
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 predicted pro_longevity but the ground truth is anti_longevity. The model's reasoning is logically coherent but leads to the wrong conclusion. The model assumed that because CCT-4 is a chaperonin subunit involved in proteostasis, it must be pro-longevity (i.e., its loss would reduce lifespan). However, the GenAge database classifies cct-4 as anti_longevity, meaning its activity actually reduces lifespan (or its loss extends lifespan). This is consistent with findings in C. elegans where RNAi knockdown of TRiC/CCT subunits can extend lifespan, possibly by activating stress response pathways or reducing translation/folding of pro-aging proteins. The model's mechanistic reasoning about proteostasis is generally sound but it made the wrong directional inference about whether CCT-4 promotes or opposes longevity. The confidence of 0.72 is notably high for an incorrect prediction.
Raw API responses
solver
{
"reasoning": "CCT-4 is the delta subunit of the TRiC/CCT chaperonin complex, which uses ATP hydrolysis to fold nascent and misfolded proteins into their native conformations. Proper proteostasis is a well-established determinant of longevity in C. elegans, and TRiC/CCT activity directly prevents the accumulation of misfolded and aggregated proteins that drive aging pathology. The complex is known to assist folding of cytoskeletal proteins (actin, tubulin) and other essential substrates, and its activity intersects with the broader HSP90/HSP70 chaperone network that supports stress resistance and lifespan. Loss of CCT subunit function in C. elegans leads to proteotoxic stress and reduced fitness, while maintenance of chaperonin capacity supports healthy aging by counteracting protein aggregation, a hallmark of age-related decline.",
"confidence": 0.72,
"key_pathways": [
"TRiC/CCT chaperonin-mediated protein folding",
"proteostasis network",
"ATP-dependent chaperone activity"
],
"mechanism_class": "loss_of_proteostasis",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model predicted pro_longevity but the ground truth is anti_longevity. The model's reasoning is logically coherent but leads to the wrong conclusion. The model assumed that because CCT-4 is a chaperonin subunit involved in proteostasis, it must be pro-longevity (i.e., its loss would reduce lifespan). However, the GenAge database classifies cct-4 as anti_longevity, meaning its activity actually reduces lifespan (or its loss extends lifespan). This is consistent with findings in C. elegans where RNAi knockdown of TRiC/CCT subunits can extend lifespan, possibly by activating stress response pathways or reducing translation/folding of pro-aging proteins. The model's mechanistic reasoning about proteostasis is generally sound but it made the wrong directional inference about whether CCT-4 promotes or opposes longevity. The confidence of 0.72 is notably high for an incorrect prediction.",
"failure_mode": "confident_wrong",
"answer_correct": false,
"mechanism_correct": false,
"reasoning_quality": 3,
"ground_truth_questionable": false
}