OMA1 hydrolyzes YME1L1

Stable Identifier
R-HSA-9840564
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Depletion of ATP and depolarization of the mitochondrial inner membrane cause degradation of YME1L1 by OMA1 (Rainbolt et al. 2015, Rainbolt et al. 2016). Oxidative stress, such as hydrogen peroxide, alters the conformation of YME1L1 which may render it susceptible to degradation by OMA1 (Brambley et al. 2019). Depolarization of the mitochondrial inner membrane also causes YME1L1 to reciprocally degrade OMA1 (Rainbolt et al. 2016).
Literature References
PubMed ID Title Journal Year
25433032 YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress

Wiseman, RL, Saunders, JM, Rainbolt, TK

EMBO Rep 2015
26923599 Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress

Wiseman, RL, Puchades, C, Rainbolt, TK, Lebeau, J

Cell Rep 2016
Participants
Participates
Catalyst Activity

metalloendopeptidase activity of OMA1(144-447):Zn2+ [mitochondrial inner membrane]

This event is regulated
Negatively by
Orthologous Events
Authored
Reviewed
Created
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