Results 51 to 60 of about 22,170 (231)

Oxidization of optic atrophy 1 cysteines occurs during heart ischemia-reperfusion and amplifies cell death by oxidative stress

Redox Biology, 2023
During cardiac ischemia-reperfusion, excess reactive oxygen species can damage mitochondrial, cellular and organ function. Here we show that cysteine oxidation of the mitochondrial protein Opa1 contributes to mitochondrial damage and cell death caused by
Martina Semenzato, Mark J. Kohr, Charlotte Quirin, Roberta Menabò, Petra Alanova, Lukas Alan, Anna Pellattiero, Elizabeth Murphy, Fabio Di Lisa, Luca Scorrano   +9 more
doaj   +1 more source

Natural and Induced Mitochondrial Phosphate Carrier Loss: DIFFERENTIAL DEPENDENCE OF MITOCHONDRIAL METABOLISM AND DYNAMICS AND CELL SURVIVAL ON THE EXTENT OF DEPLETION. [PDF]

, 2016
The relevance of mitochondrial phosphate carrier (PiC), encoded by SLC25A3, in bioenergetics is well accepted. However, little is known about the mechanisms mediating the cellular impairments induced by pathological SLC25A3 variants.
Acoba, Michelle G., Anderson-Pullinger, Lauren, Claypool, Steven M., Golenár, Tünde, Gál, Aniko, Hajnóczky, György, Li, Qipei, Moffat, Cynthia, Seifert, Erin L., Sondheimer, Neal   +9 more
core   +2 more sources

Autosomal dominant optic atrophy: A novel treatment for OPA1 splice defects using U1 snRNA adaption

Molecular Therapy: Nucleic Acids, 2021
Autosomal dominant optic atrophy (ADOA) is frequently caused by mutations in the optic atrophy 1 (OPA1) gene, with haploinsufficiency being the major genetic pathomechanism. Almost 30% of the OPA1-associated cases suffer from splice defects.
Christoph Jüschke, Thomas Klopstock, Claudia B. Catarino, Marta Owczarek-Lipska, Bernd Wissinger, John Neidhardt   +5 more
doaj   +1 more source

Mitochondrial fusion and Bid-mediated mitochondrial apoptosis are perturbed by alcohol with distinct dependence on its metabolism [PDF]

, 2018
Environmental stressors like ethanol (EtOH) commonly target mitochondria to influence the cell’s fate. Recent literature supports that chronic EtOH exposure suppresses mitochondrial dynamics, central to quality control, and sensitizes mitochondrial ...
Hajnóczky, György, Madesh, Muniswamy, Naghdi, Shamim, Rubin, Emanual, Slovinsky, William S.   +4 more
core   +3 more sources

Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion [PDF]

, 2009
Two dynamin-related protein (DRP) families are essential for fusion of the outer and inner mitochondrial membranes, Fzo1 (yeast)/Mfn1/Mfn2 (mammals) and Mgm1 (yeast)/Opa1 (mammals), respectively.
Rachel M. DeVay, Lenin Dominguez-Ramirez, Laura L. Lackner, Suzanne Hoppins, Henning Stahlberg, Jodi Nunnari, Cipolat, Crowther, Danino, Daum, Duvezin-Caubet, Esser, Frezza, Gasper, Gipson, Gipson, Gray, Griffin, Griparic, Herlan, Herlan, Hermann, Hoppins, Hoppins, Ingerman, Ishihara, Ishihara, Koshiba, Lassmann, Lévy, Longtine, Low, Martí-Renom, McGuffin, McQuibban, Meeusen, Meeusen, Meglei, Naylor, Pettersen, Quan, Ramachandran, Rapaport, Siegel, Sesaki, Song, Sperka-Gottlieb, Tovchigrechko, Wong, Zick, Zinser   +50 more
core   +2 more sources

What is the function of mitochondrial networks? A theoretical assessment of hypotheses and proposal for future research [PDF]

, 2015
Mitochondria can change their shape from discrete isolated organelles to a large continuous reticulum. The cellular advantages underlying these fused networks are still incompletely understood.
Ainscow, Amchenkova, Bakeeva, Bazil, Beard, Bernardi, Brand, Braschi, Busch, Cagalinec, Castanier, Chan, Chen, Chen, Chen, Chouhan, Cipolat, Cortassa, das Neves, De Marchi, Dedkova, Denton, Denton, Ehses, Estaquier, Figge, Fischer, Frezza, Friedman, Gilkerson, Gilkerson, Gomes, Gottlieb, Grandemange, Groen, Harrison, Head, Hemion, Imai, Jahani-Asl, Jahani-Asl, Jimenez, Johnston, Johnston, Junesch, Kim, Kowald, Krapivsky, Laar, Lee, Legros, Lemasters, Liesa, Liu, Liu, Logan, Magnus, Mai, Malli, Maltecca, McBride, McCormack, Meeusen, Mishra, Mitra, Mitra, Mouli, Murphy, Nakada, Narendra, Neuspiel, Olichon, Ong, Ono, Parone, Partikian, Patel, Patergnani, Patten, Picard, Picard, Qian, Rafelski, Rafelski, Rambold, Rizzuto, Rizzuto, Rodell, Rolland, Saa, Sahimi, Skulachev, Skulachev, Soboll, Soga, Song, Soubannier, Stauffer, Sukhorukov, Szabadkai, Tondera, Twig, Twig, van der Bliek, Verkman, Vinnakota, Viola, Wan, Westrate, Wikstrom, Wikstrom, Wilkens, Wu, Wu, Youle, Zemirli, Zhang, Zhu   +117 more
core   +2 more sources

Disruption of fusion results in mitochondrial heterogeneity and dysfunction [PDF]

, 2005
Mitochondria undergo continual cycles of fusion and fission, and the balance of these opposing processes regulates mitochondrial morphology. Paradoxically, cells invest many resources to maintain tubular mitochondrial morphology, when reducing both ...
Chan, David C., Chen, Hsiuchen, Chomyn, Anne   +2 more
core   +2 more sources

Structure and function of bacterial dynamin-like proteins [PDF]

, 2012
Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis
Bramkamp, Marc
core   +1 more source

The dynamin GTPase OPA1: More than mitochondria?

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013
The studies addressing the molecular mechanisms governing mitochondrial fusion and fission have brought to light a small group of dynamin-like GTPases (Guanosine-Triphosphate hydrolase) as central regulators of mitochondrial morphology and cristae remodeling, apoptosis, calcium signaling, and metabolism. One of them is the mammalian OPA1 (Optic atrophy
Belenguer, Pascale, Pellegrini, Luca
openaire   +2 more sources

SIRT4 positively regulates autophagy via ULK1, but independently of HDAC6 and OPA1

FEBS Open Bio, EarlyView.
Cells expressing SIRT4 (H161Y), a catalytically inactive mutant of the sirtuin SIRT4, fail to upregulate LC3B‐II and exhibit a reduced autophagic flux under stress conditions. Interestingly, SIRT4(H161Y) promotes phosphorylation of ULK1 at S638 and S758 that are associated with inhibition of autophagy initiation.
Isabell Lehmkuhl, Khawar Amin, Lydia Gabriel, Nils Hampel, Afshin Iram, Julia Hesse, Constanze Wiek, Jasmin Thuy Vy Nguyen, Helmut Hanenberg, Jürgen Scheller, M. Reza Ahmadian, Björn Stork, Doreen M. Floss, Roland P. Piekorz   +13 more
wiley   +1 more source