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Literature summary for 3.4.24.B19 extracted from

  • Rainbolt, T.K.; Saunders, J.M.; Wiseman, R.L.
    YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress (2015), EMBO Rep., 16, 97-106.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in SHSY5Y cells Saccharomyces cerevisiae

General Stability

General Stability Organism
YME1L is a stress-sensitive mitochondrial protease that is rapidly degraded in response to acute oxidative (0.2 mM H2O2) stress Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane inner mitochondrial membrane Saccharomyces cerevisiae 31966
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae YME1L degradation involves the activity of the ATP-independent mitochondrial protease OMA1 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information YME1L degradation involves the activity of the ATP-independent mitochondrial protease OMA1 Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Yme1L
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function stress-induced YME1L degradation attenuates protective regulation of mitochondrial proteostasis and promotes cellular death in response to oxidative stress Saccharomyces cerevisiae