lbp-8
C. elegans
Fatty acid-binding protein homolog 8
What the model saw
Gene: lbp-8 Organism: Caenorhabditis elegans Known functions: Fatty acid-binding protein homolog 8. fatty acid binding. lipid binding. long-chain fatty acid binding. long-chain fatty acid transmembrane transporter activity. oleic acid binding.
View unredacted entry
Fatty acid-binding protein homolog 8. fatty acid binding. lipid binding. long-chain fatty acid binding. long-chain fatty acid transmembrane transporter activity. oleic acid binding.
Solver output
LBP-8 is a fatty acid-binding protein (FABP) homolog in C. elegans that binds long-chain fatty acids, including oleic acid, and facilitates their intracellular transport and trafficking. FABPs in C. elegans have been shown to act as lipid chaperones that shuttle fatty acid ligands to nuclear receptors (such as NHR-49, the C. elegans PPARα homolog), thereby modulating lipid metabolism and nutrient-sensing transcriptional programs. Oleic acid binding is particularly relevant because oleic acid is a key signaling lipid that activates nuclear hormone receptors linked to fat oxidation and longevity pathways. Proper intracellular lipid trafficking via LBP-8 supports healthy lipid homeostasis and mitochondrial fatty acid oxidation, processes that are tightly coupled to lifespan extension in C. elegans. Disruption of lipid-sensing and fatty acid transport in worms is associated with shortened lifespan, while enhanced flux through these pathways (e.g., via dietary restriction or fat oxidation) promotes longevity.
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 lbp-8 as pro_longevity with reasonable confidence (0.72). The mechanistic reasoning is well-grounded: lbp-8 encodes a fatty acid-binding protein that binds oleic acid and long-chain fatty acids, and the model correctly identifies the connection to nuclear hormone receptor signaling (NHR-49/PPARα) and lipid homeostasis pathways relevant to C. elegans longevity. The mechanism class "deregulated_nutrient_sensing" is a reasonable categorization, though lipid transport/signaling might be more precise. The reasoning about FABPs shuttling fatty acids to nuclear receptors is biologically plausible and consistent with published literature on C. elegans LBPs. Overall a solid prediction with good mechanistic reasoning.
Raw API responses
solver
{
"reasoning": "LBP-8 is a fatty acid-binding protein (FABP) homolog in C. elegans that binds long-chain fatty acids, including oleic acid, and facilitates their intracellular transport and trafficking. FABPs in C. elegans have been shown to act as lipid chaperones that shuttle fatty acid ligands to nuclear receptors (such as NHR-49, the C. elegans PPARα homolog), thereby modulating lipid metabolism and nutrient-sensing transcriptional programs. Oleic acid binding is particularly relevant because oleic acid is a key signaling lipid that activates nuclear hormone receptors linked to fat oxidation and longevity pathways. Proper intracellular lipid trafficking via LBP-8 supports healthy lipid homeostasis and mitochondrial fatty acid oxidation, processes that are tightly coupled to lifespan extension in C. elegans. Disruption of lipid-sensing and fatty acid transport in worms is associated with shortened lifespan, while enhanced flux through these pathways (e.g., via dietary restriction or fat oxidation) promotes longevity.",
"confidence": 0.72,
"key_pathways": [
"NHR-49/PPARα nuclear hormone receptor lipid signaling",
"long-chain fatty acid intracellular transport and oxidation",
"lipid homeostasis and nutrient sensing"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted lbp-8 as pro_longevity with reasonable confidence (0.72). The mechanistic reasoning is well-grounded: lbp-8 encodes a fatty acid-binding protein that binds oleic acid and long-chain fatty acids, and the model correctly identifies the connection to nuclear hormone receptor signaling (NHR-49/PPARα) and lipid homeostasis pathways relevant to C. elegans longevity. The mechanism class \"deregulated_nutrient_sensing\" is a reasonable categorization, though lipid transport/signaling might be more precise. The reasoning about FABPs shuttling fatty acids to nuclear receptors is biologically plausible and consistent with published literature on C. elegans LBPs. Overall a solid prediction with good mechanistic reasoning.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}