Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Combined Automated Annotation using Multiple IEA Methods
The C. elegans Opa1 homologue EAT-3 is essential for resistance to free radicals.
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EAT-3 is the C. elegans ortholog of OPA1/Mgm1, with conserved dynamin domains
"Similar to yeast Mgm1 and mammalian Opa1, this C. elegans protein has a putative mitochondrial targeting sequence followed by domains that are typical of dynamin family members: a conserved GTPase domain, a middle domain and a GED or assembly domain"
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eat-3 mutations cause mitochondrial fragmentation with inner membrane septae
"We find that mutations in the C. elegans eat-3 locus cause mitochondria to fragment in agreement with the mutant phenotypes observed in yeast and mammalian cells. Electron microscopy shows that the matrices of fragmented mitochondria in eat-3 mutants are divided by inner membrane septae, suggestive of a specific defect in fusion of the mitochondrial inner membrane."
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Cristae length is reduced by 66.2% after normalization to inner-boundary membrane length.
"There is, however, still a 66.2% decrease of total cristae length when normalized with the lengths of inner boundary membranes or a 70.3% decrease when normalized with the surface area of the mitochondrial section."
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eat-3 mutants are hypersensitive to paraquat and induce SOD-2
"eat-3 mutants are hypersensitive to paraquat, which promotes damage by free radicals, and they are sensitive to loss of the mitochondrial superoxide dismutase sod-2. We conclude that free radicals contribute to the pathology of C. elegans eat-3 mutants."
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drp-1 mutations suppress eat-3 phenotypes
"We conclude that a functioning mitochondrial division apparatus is required for the mitochondrial fragmentation induced by mutant eat-3."
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ced-3/ced-4 mutations do not suppress eat-3 phenotypes
"Although mammalian Opa1 is antiapoptotic, mutations in the canonical C. elegans cell death genes ced-3 and ced-4 do not suppress the slow growth and small broodsize phenotypes of eat-3 mutants."
Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution pathways downstream of ced-3 and independent of ced-9.
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eat-3 and fzo-1 are not required for apoptosis activation in C. elegans
"Here we report that profusion genes fzo-1 and eat-3 or the profission gene drp-1 are not required for apoptosis activation in C. elegans."
A novel mitochondrial outer membrane protein, MOMA-1, that affects cristae morphology in Caenorhabditis elegans.
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EAT-3 co-fractionates with mitochondria (88% in mitochondrial pellet)
"The distributions were quantified with densitometry of P2 and S2 fractions: 88% of EAT-3, 12% of tubulin, and 98% of MOMA-1 is in the mitochondrial pellet."
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EAT-3 is protease-protected in intact mitochondria
"MOMA-1 is digested when no detergent is added, like MFF-1, while EAT-3 and F1β are protease protected."
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EAT-3 used as IMS marker in protease protection experiments
"antibodies against the C. elegans Opa1 homologue EAT-3 (Kanazawa et al., 2008) as a control for proteins exposed to the IMS"
Deep research review of eat-3 gene function
Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion.
Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin.
EAT-3: microtubule and peroxisome capacities
Cryo-EM structures of S-OPA1 reveal its interactions with membrane and changes upon nucleotide binding.