hsp-16.1
C. elegans
Heat shock protein Hsp-16.1/Hsp-16.11
What the model saw
Gene: hsp-16.1 Organism: Caenorhabditis elegans Known functions: Heat shock protein Hsp-16.1/Hsp-16.11. unfolded protein binding.
View unredacted entry
Heat shock protein Hsp-16.1/Hsp-16.11. unfolded protein binding.
Solver output
hsp-16.1 encodes a small heat shock protein (sHSP) in C. elegans that functions as a molecular chaperone via unfolded protein binding. By binding misfolded or aggregation-prone proteins, it prevents toxic protein aggregation and supports proteostasis — a central determinant of lifespan in C. elegans. hsp-16.1 is a well-characterized transcriptional target of the DAF-16/FOXO transcription factor downstream of the insulin/IGF-1 signaling pathway; its upregulation is strongly associated with extended lifespan in daf-2 mutants. Overexpression of hsp-16.1 has been shown to extend lifespan in C. elegans, while its loss compromises stress resistance and proteostasis. The chaperone activity directly counteracts the age-related decline in protein quality control, placing it firmly in the proteostasis hallmark of aging.
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 pro_longevity for hsp-16.1 with high confidence (0.82). The mechanistic reasoning is thorough and accurate: hsp-16.1 is indeed a small heat shock protein that functions as a molecular chaperone, is a DAF-16/FOXO transcriptional target downstream of insulin/IGF-1 signaling, and its overexpression extends lifespan in C. elegans. The identification of key pathways (insulin/IGF-1 signaling, proteostasis/chaperone network, heat shock response) is all correct and well-supported by the literature.
Raw API responses
solver
{
"reasoning": "hsp-16.1 encodes a small heat shock protein (sHSP) in C. elegans that functions as a molecular chaperone via unfolded protein binding. By binding misfolded or aggregation-prone proteins, it prevents toxic protein aggregation and supports proteostasis — a central determinant of lifespan in C. elegans. hsp-16.1 is a well-characterized transcriptional target of the DAF-16/FOXO transcription factor downstream of the insulin/IGF-1 signaling pathway; its upregulation is strongly associated with extended lifespan in daf-2 mutants. Overexpression of hsp-16.1 has been shown to extend lifespan in C. elegans, while its loss compromises stress resistance and proteostasis. The chaperone activity directly counteracts the age-related decline in protein quality control, placing it firmly in the proteostasis hallmark of aging.",
"confidence": 0.82,
"key_pathways": [
"insulin/IGF-1 signaling (DAF-2/DAF-16 axis)",
"proteostasis / chaperone network",
"heat shock response"
],
"mechanism_class": "loss_of_proteostasis",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted pro_longevity for hsp-16.1 with high confidence (0.82). The mechanistic reasoning is thorough and accurate: hsp-16.1 is indeed a small heat shock protein that functions as a molecular chaperone, is a DAF-16/FOXO transcriptional target downstream of insulin/IGF-1 signaling, and its overexpression extends lifespan in C. elegans. The identification of key pathways (insulin/IGF-1 signaling, proteostasis/chaperone network, heat shock response) is all correct and well-supported by the literature.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}