cct-1
C. elegans
T-complex protein 1 subunit alpha
What the model saw
Gene: cct-1 Organism: Caenorhabditis elegans Known functions: T-complex protein 1 subunit alpha. ATP binding. ATP hydrolysis activity. ATP-dependent protein folding chaperone. unfolded protein binding.
View unredacted entry
T-complex protein 1 subunit alpha. ATP binding. ATP hydrolysis activity. ATP-dependent protein folding chaperone. unfolded protein binding.
Solver output
cct-1 encodes the alpha subunit of the TRiC/CCT chaperonin complex, which uses ATP hydrolysis to fold nascent and stress-denatured proteins. Proper proteostasis is a well-established determinant of longevity in C. elegans; TRiC/CCT directly folds cytoskeletal proteins (e.g., actin, tubulin) and other aggregation-prone substrates, preventing toxic protein aggregation. Loss of TRiC/CCT function accelerates proteotoxic stress and is associated with shortened lifespan, while its activity supports the proteostasis network that declines with age. The ATP-dependent chaperone activity of CCT-1 is central to maintaining the soluble proteome, placing it squarely within the proteostasis hallmark of aging. Enhanced or sustained TRiC/CCT activity has been linked to improved protein quality control and extended healthspan in invertebrate models.
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 assumes that because CCT-1 is a chaperone supporting proteostasis, it must be pro-longevity (i.e., its loss shortens lifespan). However, the GenAge database classifies cct-1 as anti_longevity, meaning its reduction/loss actually 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 the folding of proteins that promote aging. The model's mechanistic reasoning is also incorrect — it assumes the gene promotes longevity by maintaining proteostasis, but the actual finding is the opposite. The model was fairly confident (0.75) in its wrong answer.
Raw API responses
solver
{
"reasoning": "cct-1 encodes the alpha subunit of the TRiC/CCT chaperonin complex, which uses ATP hydrolysis to fold nascent and stress-denatured proteins. Proper proteostasis is a well-established determinant of longevity in C. elegans; TRiC/CCT directly folds cytoskeletal proteins (e.g., actin, tubulin) and other aggregation-prone substrates, preventing toxic protein aggregation. Loss of TRiC/CCT function accelerates proteotoxic stress and is associated with shortened lifespan, while its activity supports the proteostasis network that declines with age. The ATP-dependent chaperone activity of CCT-1 is central to maintaining the soluble proteome, placing it squarely within the proteostasis hallmark of aging. Enhanced or sustained TRiC/CCT activity has been linked to improved protein quality control and extended healthspan in invertebrate models.",
"confidence": 0.75,
"key_pathways": [
"TRiC/CCT chaperonin-mediated protein folding",
"proteostasis network",
"cytoskeletal protein biogenesis"
],
"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 assumes that because CCT-1 is a chaperone supporting proteostasis, it must be pro-longevity (i.e., its loss shortens lifespan). However, the GenAge database classifies cct-1 as anti_longevity, meaning its reduction/loss actually 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 the folding of proteins that promote aging. The model's mechanistic reasoning is also incorrect — it assumes the gene promotes longevity by maintaining proteostasis, but the actual finding is the opposite. The model was fairly confident (0.75) in its wrong answer.",
"failure_mode": "confident_wrong",
"answer_correct": false,
"mechanism_correct": false,
"reasoning_quality": 2,
"ground_truth_questionable": false
}