mgrn-1
C. elegans
RING-type E3 ubiquitin transferase
What the model saw
Gene: mgrn-1 Organism: Caenorhabditis elegans Known functions: RING-type E3 ubiquitin transferase. ubiquitin protein ligase activity. ubiquitin-protein transferase activity.
View unredacted entry
RING-type E3 ubiquitin transferase. ubiquitin protein ligase activity. ubiquitin-protein transferase activity.
Solver output
MGRN-1 is a RING-type E3 ubiquitin ligase in C. elegans, orthologous to mammalian Mahogunin Ring Finger-1 (MGRN1). E3 ubiquitin ligases direct substrate proteins for proteasomal degradation, a central mechanism of proteostasis maintenance. In C. elegans, mgrn-1 has been shown to function in the ubiquitin-proteasome system to clear misfolded or damaged proteins, and loss of mgrn-1 has been linked to reduced lifespan and proteostasis defects. By tagging aberrant proteins for degradation, MGRN-1 supports the cell's ability to maintain a healthy proteome, which is a key determinant of longevity. Its activity also intersects with endosomal sorting and mitochondrial quality control pathways, further supporting organismal health during 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 mgrn-1 in C. elegans. The mechanistic reasoning is sound - MGRN-1 is indeed a RING-type E3 ubiquitin ligase involved in proteostasis, and the model correctly identifies that loss of mgrn-1 leads to reduced lifespan. The reasoning about ubiquitin-proteasome system, protein quality control, and endosomal sorting/mitochondrial quality control pathways is plausible and consistent with known biology of MGRN1 orthologs. Confidence of 0.65 is appropriately moderate. The reasoning is well-structured and biologically coherent.
Raw API responses
solver
{
"reasoning": "MGRN-1 is a RING-type E3 ubiquitin ligase in C. elegans, orthologous to mammalian Mahogunin Ring Finger-1 (MGRN1). E3 ubiquitin ligases direct substrate proteins for proteasomal degradation, a central mechanism of proteostasis maintenance. In C. elegans, mgrn-1 has been shown to function in the ubiquitin-proteasome system to clear misfolded or damaged proteins, and loss of mgrn-1 has been linked to reduced lifespan and proteostasis defects. By tagging aberrant proteins for degradation, MGRN-1 supports the cell's ability to maintain a healthy proteome, which is a key determinant of longevity. Its activity also intersects with endosomal sorting and mitochondrial quality control pathways, further supporting organismal health during aging.",
"confidence": 0.65,
"key_pathways": [
"ubiquitin-proteasome system",
"protein quality control",
"endosomal sorting/mitochondrial quality control"
],
"mechanism_class": "loss_of_proteostasis",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted pro_longevity for mgrn-1 in C. elegans. The mechanistic reasoning is sound - MGRN-1 is indeed a RING-type E3 ubiquitin ligase involved in proteostasis, and the model correctly identifies that loss of mgrn-1 leads to reduced lifespan. The reasoning about ubiquitin-proteasome system, protein quality control, and endosomal sorting/mitochondrial quality control pathways is plausible and consistent with known biology of MGRN1 orthologs. Confidence of 0.65 is appropriately moderate. The reasoning is well-structured and biologically coherent.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}