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Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Additionally we are shipping OMA1 Antibodies (8) and and many more products for this protein.
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stress-induced OMA1 activation and guanosine triphosphatase OPA1 cleavage limit mitochondrial fusion and promote neuronal death
The IMQC protease Oma1 is required for the stability of the respiratory supercomplexes and thus balanced and tunable bioenergetic function.
OMA1-mediated OPA1 proteolysis plays an important role in the disruption of mitochondrial dynamics in ischemic acute kidney injury.
Constitutive OPA1 cleavage by YME1L (show YME1L1 Proteins) and OMA1 at two distinct sites leads to the accumulation of both long and short forms of OPA1 and maintains mitochondrial fusion.
Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics.
This study shows that OMA1 plays an essential role in the proteolytic inactivation of the dynamin (show DNM1 Proteins)-related GTPase (show RACGAP1 Proteins) OPA1 and describes its unexpected role in energy metabolism
OMA1 regulates OPA1 cleavage in the mitochondrial inner membrane.
The mitochondrial metalloprotease (show ADAM8 Proteins) OMA1 was activated in a Bax (show BAX Proteins)- and Bak (show BAK1 Proteins)-dependent fashion.
Cleavage of the inner membrane fusion factor L-OPA1 (show OPA1 Proteins) is prevented due to the failure to activate the inner membrane protease OMA1 in mitochondria that have a collapsed membrane potential.
OMA1 is cleaved to a short form (S-OMA1) by itself upon mitochondrial membrane depolarization; S-OMA1 is degraded quickly but could be stabilized by CCCP treatment or Prohibitin (show PHB Proteins) knockdown in cells.
These findings demonstrate that (a) p53 (show TP53 Proteins) and Oma1 mediate L-Opa1 (show OPA1 Proteins) processing, (b) mitochondrial fragmentation is involved in CDDP-induced apoptosis in OVCA and CECA cells, and (c) dysregulated mitochondrial dynamics
OMA1 controls OPA1 (show OPA1 Proteins) cleavage and function.
These results provide evidence for different substrate specificities of m-AAA (show APP Proteins) proteases composed of different subunits and reveal a striking evolutionary switch of proteases involved in the proteolytic processing of dynamin (show DNM1 Proteins)-like GTPases in mitochondria.
Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions (By similarity).
OMA1 homolog, zinc metallopeptidase
, metalloendopeptidase OMA1, mitochondrial
, overlapping with the m-AAA protease 1 homolog
, OMA1 zinc metallopeptidase homolog
, metalloprotease related protein 1
, metalloprotease-related protein 1
, overlapping activity with M-AAA protease
, zinc metallopeptidase OMA1