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Literature summary for 3.4.24.B18 extracted from

  • Volonte, D.; Liu, Z.; Shiva, S.; Galbiati, F.
    Caveolin-1 controls mitochondrial function through regulation of m-AAA mitochondrial protease (2016), Aging, 8, 2355-2369 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B18

Protein Variants

Protein Variants Comment Organism
additional information in a mutant form of AFG3L2, in which the aromatic residues within the caveolin-1-binding domain are substituted with alanines, the interaction with caveolin-1 is dramatically compromised Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Mus musculus 5739
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast embryonic fibroblast Mus musculus
-

Synonyms

Synonyms Comment Organism
AFG3-like protein 2
-
 Mus musculus
AFG3L2
-
 Mus musculus

General Information

General Information Comment Organism
physiological function protease AFG3L2 is a caveolin-1-interacting protein in vitro. Oxidative stress promotes the translocation of both caveolin-1 and AFG3L2 to mitochondria, enhances the interaction of caveolin-1 with AFG3L2 in mitochondria and stimulates mitochondrial protease activity in wild-type fibroblasts. Localization of AFG3L2 to mitochondria after oxidative stress is inhibited in fibroblasts lacking caveolin-1, which results in impaired mitochondrial protein quality control, an oxidative phosphorylation to aerobic glycolysis switch and reduced ATP production. Expression of a mutant form of AFG3L2 with reduced affinity for caveolin-1, fails to localize to mitochondria and promotes degradation of complex IV after oxidative stress Mus musculus