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ALG6

S. cerevisiae

dolichyl-P-Glc:Man(9)GlcNAc(2)-PP-dolichol alpha-1,3-glucosyltransferase

What the model saw

Gene: ALG6
Organism: Saccharomyces cerevisiae
Known functions: dolichyl-P-Glc:Man(9)GlcNAc(2)-PP-dolichol alpha-1,3-glucosyltransferase. dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity. hexosyltransferase activity.
View unredacted entry
dolichyl-P-Glc:Man(9)GlcNAc(2)-PP-dolichol alpha-1,3-glucosyltransferase. dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity. hexosyltransferase activity.

Solver output

Predicted influence
Pro-longevity
Confidence
65%
Mechanism
Loss of proteostasis
Reasoning

ALG6 encodes the dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase, which catalyzes the first glucosylation step in the N-glycan precursor assembly pathway on the ER membrane. This glucosylation is essential for the completion of the Glc3Man9GlcNAc2-PP-dolichol lipid-linked oligosaccharide that is transferred en bloc to nascent polypeptides by the oligosaccharyltransferase complex. Proper N-glycosylation is required for correct protein folding, ER quality control (via the calnexin/calreticulin cycle), and ERAD-mediated clearance of misfolded proteins. Loss of ALG6 function leads to hypoglycosylation, accumulation of misfolded glycoproteins, and ER stress, which are hallmarks of impaired proteostasis and are associated with accelerated aging. Therefore, the normal function of ALG6 supports proteostasis by ensuring proper glycoprotein folding and quality control, promoting longevity.

Key pathways
N-linked glycosylation / dolichol-linked oligosaccharide assemblyER protein quality control and unfolded protein response (UPR)Proteostasis and ERAD
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 but the ground truth is anti_longevity. The model's reasoning assumes that because ALG6 supports proteostasis and proper glycoprotein folding, its normal function must promote longevity. However, in yeast longevity studies, genes classified as anti_longevity are typically those whose deletion extends lifespan. ALG6 appears to be anti_longevity, meaning its loss (deletion) extends lifespan rather than shortening it. The model's mechanistic reasoning about N-glycosylation and proteostasis is plausible in general terms but leads to the wrong conclusion about the direction of longevity influence. The model failed to consider that ER stress pathways and N-glycosylation machinery can sometimes limit lifespan, and that deletion of ALG6 may activate beneficial stress responses (like mild UPR/hormesis) that extend lifespan in yeast. The confidence of 0.65 is moderately high for an incorrect answer.

Raw API responses

solver

{
  "reasoning": "ALG6 encodes the dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase, which catalyzes the first glucosylation step in the N-glycan precursor assembly pathway on the ER membrane. This glucosylation is essential for the completion of the Glc3Man9GlcNAc2-PP-dolichol lipid-linked oligosaccharide that is transferred en bloc to nascent polypeptides by the oligosaccharyltransferase complex. Proper N-glycosylation is required for correct protein folding, ER quality control (via the calnexin/calreticulin cycle), and ERAD-mediated clearance of misfolded proteins. Loss of ALG6 function leads to hypoglycosylation, accumulation of misfolded glycoproteins, and ER stress, which are hallmarks of impaired proteostasis and are associated with accelerated aging. Therefore, the normal function of ALG6 supports proteostasis by ensuring proper glycoprotein folding and quality control, promoting longevity.",
  "confidence": 0.65,
  "key_pathways": [
    "N-linked glycosylation / dolichol-linked oligosaccharide assembly",
    "ER protein quality control and unfolded protein response (UPR)",
    "Proteostasis and ERAD"
  ],
  "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 ALG6 supports proteostasis and proper glycoprotein folding, its normal function must promote longevity. However, in yeast longevity studies, genes classified as anti_longevity are typically those whose deletion extends lifespan. ALG6 appears to be anti_longevity, meaning its loss (deletion) extends lifespan rather than shortening it. The model's mechanistic reasoning about N-glycosylation and proteostasis is plausible in general terms but leads to the wrong conclusion about the direction of longevity influence. The model failed to consider that ER stress pathways and N-glycosylation machinery can sometimes limit lifespan, and that deletion of ALG6 may activate beneficial stress responses (like mild UPR/hormesis) that extend lifespan in yeast. The confidence of 0.65 is moderately high for an incorrect answer.",
  "failure_mode": "confident_wrong",
  "answer_correct": false,
  "mechanism_correct": false,
  "reasoning_quality": 2,
  "ground_truth_questionable": false
}