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Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Zusätzlich bieten wir Ihnen OMA1 Antikörper (11) und OMA1 Kits (3) und viele weitere Produktgruppen zu diesem Protein an.
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differential stress-induced degradation of YME1L (zeige YME1L1 Proteine) and OMA1 as a mechanism for sensitively adapting mitochondrial inner membrane protease activity and function in response to distinct types of cellular insults.
The mitochondrial metalloprotease OMA1 was activated in a Bax (zeige BAX Proteine)- and Bak (zeige BAK1 Proteine)-dependent fashion.
Cleavage of the inner membrane fusion factor L-OPA1 (zeige OPA1 Proteine) 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 (zeige PHB Proteine) knockdown in cells.
These findings demonstrate that (a) p53 (zeige TP53 Proteine) and Oma1 mediate L-Opa1 (zeige OPA1 Proteine) processing, (b) mitochondrial fragmentation is involved in CDDP-induced apoptosis in OVCA and CECA cells, and (c) dysregulated mitochondrial dynamics
OMA1 controls OPA1 (zeige OPA1 Proteine) cleavage and function.
These results provide evidence for different substrate specificities of m-AAA (zeige APP Proteine) proteases composed of different subunits and reveal a striking evolutionary switch of proteases involved in the proteolytic processing of dynamin (zeige DNM1 Proteine)-like GTPases in mitochondria.
The m-AAA (zeige AAAS Proteine) protease associated with neurodegeneration limits MCU (zeige MCU Proteine) activity in mitochondria.
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 (zeige YME1L1 Proteine) 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 (zeige DNM1 Proteine)-related GTPase (zeige RACGAP1 Proteine) OPA1 and describes its unexpected role in energy metabolism
OMA1 regulates OPA1 cleavage in the mitochondrial inner membrane.
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
, OMA1 zinc metallopeptidase homolog
, metalloendopeptidase OMA1, mitochondrial
, metalloprotease related protein 1
, metalloprotease-related protein 1
, overlapping activity with M-AAA protease
, overlapping with the m-AAA protease 1 homolog
, zinc metallopeptidase OMA1
, Metalloendopeptidase OMA1, mitochondrial
, OMA1 zinc metallopeptidase
, Overlapping with the m-AAA protease 1 homolog
, Metalloendopeptidase OMA1, mitochondrial-like protein
, metalloendopeptidase OMA1 mitochondrial-like protein