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cct-8

C. elegans

CCT-theta;T-complex protein 1 subunit theta

What the model saw

Gene: cct-8
Organism: Caenorhabditis elegans
Known functions: CCT-theta;T-complex protein 1 subunit theta. ATP binding. ATP hydrolysis activity. ATP-dependent protein folding chaperone. unfolded protein binding.
View unredacted entry
CCT-theta;T-complex protein 1 subunit theta. ATP binding. ATP hydrolysis activity. ATP-dependent protein folding chaperone. unfolded protein binding.

Solver output

Predicted influence
Pro-longevity
Confidence
82%
Mechanism
Loss of proteostasis
Reasoning

CCT-8 is the theta subunit of the TRiC/CCT chaperonin complex, which uses ATP hydrolysis to fold nascent and misfolded proteins in an ATP-dependent manner. Maintenance of proteostasis is a key determinant of longevity in C. elegans, and the TRiC/CCT complex is a central node in this network, assisting in the folding of ~10% of the proteome including cytoskeletal and cell-cycle proteins. In C. elegans, overexpression of TRiC/CCT subunits has been shown to suppress protein aggregation and extend lifespan, while loss of function accelerates proteotoxic stress and shortens lifespan. By binding unfolded proteins and catalyzing their correct folding via ATP hydrolysis, CCT-8 directly opposes the accumulation of misfolded/aggregated proteins that drive aging pathology. This places cct-8 squarely within the proteostasis hallmark of aging, acting pro-longevity through the TRiC chaperonin-mediated protein quality control pathway.

Key pathways
TRiC/CCT chaperonin complex-mediated protein foldingproteostasis network / protein quality controlATP-dependent chaperone activity
Longevity influence
Anti-longevity
Lifespan effect
Increase

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

Answer
Incorrect
Mechanism
Incorrect
Reasoning quality
2/5
Failure mode
Confident wrong
Notes

The model predicted pro_longevity with high confidence (0.82), but the ground truth is anti_longevity. The model's reasoning about TRiC/CCT chaperonin complex and proteostasis is generally sound in principle, but it incorrectly applied the direction of effect. The model claimed that "overexpression of TRiC/CCT subunits has been shown to suppress protein aggregation and extend lifespan" — this appears to be a hallucinated or misapplied specific claim. In reality, cct-8 in C. elegans is classified as anti_longevity, meaning its activity (or overexpression) reduces lifespan, or its loss extends lifespan. The model's mechanistic framework about proteostasis is partially relevant but the directional conclusion is wrong. The model was confidently incorrect, which is a significant failure.

Raw API responses

solver

{
  "reasoning": "CCT-8 is the theta subunit of the TRiC/CCT chaperonin complex, which uses ATP hydrolysis to fold nascent and misfolded proteins in an ATP-dependent manner. Maintenance of proteostasis is a key determinant of longevity in C. elegans, and the TRiC/CCT complex is a central node in this network, assisting in the folding of ~10% of the proteome including cytoskeletal and cell-cycle proteins. In C. elegans, overexpression of TRiC/CCT subunits has been shown to suppress protein aggregation and extend lifespan, while loss of function accelerates proteotoxic stress and shortens lifespan. By binding unfolded proteins and catalyzing their correct folding via ATP hydrolysis, CCT-8 directly opposes the accumulation of misfolded/aggregated proteins that drive aging pathology. This places cct-8 squarely within the proteostasis hallmark of aging, acting pro-longevity through the TRiC chaperonin-mediated protein quality control pathway.",
  "confidence": 0.82,
  "key_pathways": [
    "TRiC/CCT chaperonin complex-mediated protein folding",
    "proteostasis network / protein quality control",
    "ATP-dependent chaperone activity"
  ],
  "mechanism_class": "loss_of_proteostasis",
  "longevity_influence": "pro_longevity"
}

advisor

{
  "notes": "The model predicted pro_longevity with high confidence (0.82), but the ground truth is anti_longevity. The model's reasoning about TRiC/CCT chaperonin complex and proteostasis is generally sound in principle, but it incorrectly applied the direction of effect. The model claimed that \"overexpression of TRiC/CCT subunits has been shown to suppress protein aggregation and extend lifespan\" — this appears to be a hallucinated or misapplied specific claim. In reality, cct-8 in C. elegans is classified as anti_longevity, meaning its activity (or overexpression) reduces lifespan, or its loss extends lifespan. The model's mechanistic framework about proteostasis is partially relevant but the directional conclusion is wrong. The model was confidently incorrect, which is a significant failure.",
  "failure_mode": "confident_wrong",
  "answer_correct": false,
  "mechanism_correct": false,
  "reasoning_quality": 2,
  "ground_truth_questionable": false
}
cct-8 · Caenorhabditis elegans | Aging biology eval