Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice
about
Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and DiseaseSkeletal Muscle Mitochondrial Bioenergetics and Morphology in High Fat Diet Induced Obesity and Insulin Resistance: Focus on Dietary Fat SourceRegulation of the intrinsic apoptosis pathway by reactive oxygen speciesImpaired mitochondrial dynamics and bioenergetics in diabetic skeletal muscleA Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane MetallopeptidasesOma1 Links Mitochondrial Protein Quality Control and TOR Signaling To Modulate Physiological Plasticity and Cellular Stress Responses.Mitochondrial protein quality control: the mechanisms guarding mitochondrial healthThe i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fissionYME1L degradation reduces mitochondrial proteolytic capacity during oxidative stressA novel prohibitin-binding compound induces the mitochondrial apoptotic pathway through NOXA and BIM upregulationImbalanced OPA1 processing and mitochondrial fragmentation cause heart failure in miceMitochondrial division and fusion in metabolismLoss of Yme1L perturbates mitochondrial dynamics.Impaired OMA1-dependent cleavage of OPA1 and reduced DRP1 fission activity combine to prevent mitophagy in cells that are dependent on oxidative phosphorylation.Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation.Stress-triggered activation of the metalloprotease Oma1 involves its C-terminal region and is important for mitochondrial stress protection in yeastOMA1 mediates OPA1 proteolysis and mitochondrial fragmentation in experimental models of ischemic kidney injury.p53 is required for cisplatin-induced processing of the mitochondrial fusion protein L-Opa1 that is mediated by the mitochondrial metallopeptidase Oma1 in gynecologic cancersAdaptive thermogenesis in adipocytes: is beige the new brown?Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis.Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self-cleavage.Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondriaA Mitofusin-2-dependent inactivating cleavage of Opa1 links changes in mitochondria cristae and ER contacts in the postprandial liver.ROS-triggered phosphorylation of complex II by Fgr kinase regulates cellular adaptation to fuel useMitochondrial Diseases Part II: Mouse models of OXPHOS deficiencies caused by defects in regulatory factors and other components required for mitochondrial function.Implications of mitochondrial dynamics on neurodegeneration and on hypothalamic dysfunction.Metalloprotease OMA1 Fine-tunes Mitochondrial Bioenergetic Function and Respiratory Supercomplex Stability.Transcriptome Dynamics and Potential Roles of Sox6 in the Postnatal Heart.Quality control of mitochondrial protein synthesis is required for membrane integrity and cell fitness.Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology.Sabutoclax (BI97C1) and BI112D1, putative inhibitors of MCL-1, induce mitochondrial fragmentation either upstream of or independent of apoptosis.Acute exercise remodels mitochondrial membrane interactions in mouse skeletal muscle.Insulin stimulates mitochondrial fusion and function in cardiomyocytes via the Akt-mTOR-NFκB-Opa-1 signaling pathwayChanging appetites: the adaptive advantages of fuel choice.Leukocyte mitochondrial DNA copy number, anthropometric indices, and weight change in US women.Mitochondrial protein quality control in health and disease.Mitochondrial fusion and fission proteins: novel therapeutic targets for combating cardiovascular disease.A threshold of transmembrane potential is required for mitochondrial dynamic balance mediated by DRP1 and OMA1.Hormone-induced mitochondrial fission is utilized by brown adipocytes as an amplification pathway for energy expenditure.Mitochondrial dynamics in neurodegeneration.
P2860
Q26765684-87BA0974-73BE-4CA6-B497-A6F6DAA098DCQ26772781-D0FA409A-F1DE-44F2-90C6-B25EE9EC04CEQ26995793-7E09C7D0-86A2-42E4-94FE-92A54B1B94D0Q27313507-F156A649-41C6-42CA-8144-DF88FB17EDD1Q27678477-E30E53A6-4492-4626-8663-CF2EC3B390D4Q27936052-B93D7C84-CD8E-4B36-BC28-5B68B1D972DEQ28083423-9FCC4DB1-DD05-4C45-A2CF-F40B8663532BQ28235694-CEA4C753-CB32-4CE3-95D0-3EE56FCBB2B8Q28252350-F2CF2AB7-D3E5-4DEE-BB5B-2D67A074250CQ28269042-C89A62A3-F23D-4C52-B205-7687788FD6DBQ28272272-C1E7B95F-2D54-46A8-8A90-399E63E90770Q28390964-39CCDE8F-CB42-4D92-AA84-D1739CABC3D7Q30571481-14ED59D2-8A91-4494-A3BF-AC5CB10A33BEQ30578089-270EE9E7-855E-4B76-B23F-EB9D1DBDF2CBQ33599185-4827BEDF-41A9-415C-A5AA-517243B8414DQ33676633-1D9F4289-084C-46DC-95A3-09F060B71B76Q33701546-B2AFD62F-3E13-4D2B-8C63-84AECE2A3F2FQ34245099-332D3079-DFCE-427B-93B7-243EBE342F32Q34326605-98A234ED-D103-4BD3-8CEF-3C898CBB4795Q34384160-7FBF4B99-A427-46C0-ADFC-919AE37F0B12Q34407957-8A0D4FD5-BA06-46E6-A6B7-FD040904DE69Q34509729-3C8B38EE-6639-4560-84F2-1AB7AF538D9EQ34526585-30EC9D2F-E6F6-4905-97A1-A50A34AA0AF3Q34762124-24E995F8-FB68-414F-A49B-AA98FE5CA769Q35660977-3CE6BD3C-799C-408B-A127-4E08987FD228Q35708874-370B4EF3-8BA4-49CA-8A0D-1693E3E8AF0BQ36056367-BEFB331D-2BC2-4A07-86E3-A6871CB3CE6EQ36188897-ACEF23E9-7F94-4AAE-99B7-DA5614EADF42Q36210696-68AAC418-F404-4D32-BFCD-587F0406746BQ36728778-DBEFA059-8772-4223-8509-8A5A2A4627A8Q36801115-2FE37764-152D-47AB-9ED3-EEFE24BD7063Q37346132-CA42E08A-709D-4780-AC35-55F661078DB1Q37403315-7B52F4DA-D1AE-48C8-AE20-E02BE282F852Q37624803-647FA73F-6DA0-40D9-BAAD-B98D71F8AFA2Q37645083-A50A8513-33E7-44D6-AD9F-D5910C3EEE61Q37686252-F56B662E-9BA0-46EC-8C46-8A8FC1F34586Q37686255-501188C3-2A77-4606-B27F-0D61761F46DCQ37694273-812994D8-B11B-46E6-A5DB-36C40A872CA9Q37697959-FCFD2B75-7C72-4630-8E68-E0C2E5761C1FQ38060435-95EDD3A9-26F5-4B56-8471-701261C4C42F
P2860
Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Loss of mitochondrial protease ...... efective thermogenesis in mice
@ast
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en-gb
Loss of mitochondrial protease ...... efective thermogenesis in mice
@nl
type
label
Loss of mitochondrial protease ...... efective thermogenesis in mice
@ast
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en-gb
Loss of mitochondrial protease ...... efective thermogenesis in mice
@nl
prefLabel
Loss of mitochondrial protease ...... efective thermogenesis in mice
@ast
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en-gb
Loss of mitochondrial protease ...... efective thermogenesis in mice
@nl
P2093
P2860
P50
P921
P3181
P356
P1433
P1476
Loss of mitochondrial protease ...... efective thermogenesis in mice
@en
P2093
Andrew J Ramsay
Antonio Zorzano
David Sala
Francisco Rodríguez
José A Vega
Maria Soledad Fernández-García
Pedro M Quirós
P2860
P304
P3181
P356
10.1038/EMBOJ.2012.70
P407
P577
2012-03-20T00:00:00Z