phb-2
C. elegans
Mitochondrial prohibitin complex protein 2
What the model saw
Gene: phb-2 Organism: Caenorhabditis elegans Known functions: Mitochondrial prohibitin complex protein 2. protein homodimerization activity.
View unredacted entry
Mitochondrial prohibitin complex protein 2. protein homodimerization activity.
Solver output
PHB-2 is a core subunit of the mitochondrial prohibitin complex (PHB1/PHB-1 + PHB2/PHB-2 heterodimer), which forms a large ring-like scaffold in the inner mitochondrial membrane. This complex stabilizes mitochondrial membrane proteins, supports mitochondrial cristae morphology, and regulates mitochondrial fusion/fission dynamics and respiratory chain complex assembly. In C. elegans, the prohibitin complex has been shown to modulate mitochondrial function and lifespan; loss of phb-2 disrupts mitochondrial integrity and is associated with reduced longevity. The protein homodimerization activity reflects the self-assembly step required before heterodimerization with PHB-1 to form the functional complex. By maintaining mitochondrial membrane architecture and respiratory efficiency, PHB-2 opposes mitochondrial dysfunction, a key hallmark of aging, thereby promoting 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 pro_longevity for phb-2 in C. elegans with good confidence (0.72). The mechanistic reasoning is solid: PHB-2 is indeed a core subunit of the mitochondrial prohibitin complex, which forms a heterodimeric ring structure in the inner mitochondrial membrane, stabilizes mitochondrial membrane proteins, and supports cristae morphology. The model correctly notes that loss of phb-2 disrupts mitochondrial integrity and reduces longevity. The key pathways identified are appropriate. One minor note: the model mentions "protein homodimerization activity" as a step before heterodimerization, which is a reasonable interpretation of the annotated function, though the prohibitin complex is primarily known as a heterodimer (PHB-1/PHB-2). The reasoning is slightly imprecise here but not fundamentally wrong. Overall, this is a well-reasoned and correct prediction.
Raw API responses
solver
{
"reasoning": "PHB-2 is a core subunit of the mitochondrial prohibitin complex (PHB1/PHB-1 + PHB2/PHB-2 heterodimer), which forms a large ring-like scaffold in the inner mitochondrial membrane. This complex stabilizes mitochondrial membrane proteins, supports mitochondrial cristae morphology, and regulates mitochondrial fusion/fission dynamics and respiratory chain complex assembly. In C. elegans, the prohibitin complex has been shown to modulate mitochondrial function and lifespan; loss of phb-2 disrupts mitochondrial integrity and is associated with reduced longevity. The protein homodimerization activity reflects the self-assembly step required before heterodimerization with PHB-1 to form the functional complex. By maintaining mitochondrial membrane architecture and respiratory efficiency, PHB-2 opposes mitochondrial dysfunction, a key hallmark of aging, thereby promoting longevity.",
"confidence": 0.72,
"key_pathways": [
"mitochondrial prohibitin complex assembly",
"mitochondrial inner membrane integrity and cristae organization",
"mitochondrial fusion/fission dynamics"
],
"mechanism_class": "mitochondrial_dysfunction",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted pro_longevity for phb-2 in C. elegans with good confidence (0.72). The mechanistic reasoning is solid: PHB-2 is indeed a core subunit of the mitochondrial prohibitin complex, which forms a heterodimeric ring structure in the inner mitochondrial membrane, stabilizes mitochondrial membrane proteins, and supports cristae morphology. The model correctly notes that loss of phb-2 disrupts mitochondrial integrity and reduces longevity. The key pathways identified are appropriate. One minor note: the model mentions \"protein homodimerization activity\" as a step before heterodimerization, which is a reasonable interpretation of the annotated function, though the prohibitin complex is primarily known as a heterodimer (PHB-1/PHB-2). The reasoning is slightly imprecise here but not fundamentally wrong. Overall, this is a well-reasoned and correct prediction.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}