Difference between revisions of "Schlattner 2018 MiPschool Tromso B1"
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|event=MiPschool Tromso-Bergen 2018 | |event=MiPschool Tromso-Bergen 2018 | ||
|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MitoEAGLE]] | |abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MitoEAGLE]] | ||
Mitochondrial isoforms of nucleoside diphosphate kinase (NDPK-D or NME4) and creatine kinase (mtCK) are phylogenetically unrelated but share important structural and functional properties. They are both located in the intermembrane/cristae space and use mitochondrially generated ATP to phosphorylate their specific substrates, NDPs or creatine, thus regenerating ADP within the mitochondria. Both enzymes functionally interact with inner membrane adenylate translocator, thus allowing for privileged exchange (channeling) of these metabolites. We will discuss the molecular basis of this metabolite channeling and its functional consequences beyond the simple maintenance of proper nucleotide pools: stimulation of respiration, “energy export”, and regulation of ROS production, permeability transition and mitochondrial shape. | Mitochondrial isoforms of [[nucleoside diphosphate kinase]] (NDPK-D or NME4) and [[creatine kinase]] (mtCK) are phylogenetically unrelated but share important structural and functional properties. They are both located in the intermembrane/cristae space and use mitochondrially generated ATP to phosphorylate their specific substrates, [[nucleoside diphosphate |NDPs]] or [[creatine]], thus regenerating ADP within the mitochondria. Both enzymes functionally interact with inner membrane [[adenylate translocator]], thus allowing for privileged exchange (channeling) of these metabolites. We will discuss the molecular basis of this [[metabolite channeling]] and its functional consequences beyond the simple maintenance of proper [[nucleotide]] pools: stimulation of respiration, “energy export”, and regulation of ROS production, [[permeability transition]], and mitochondrial shape. | ||
|editor=[[Beno M]], [[Plangger M]] | |editor=[[Beno M]], [[Plangger M]] | ||
|mipnetlab=FR Grenoble Schlattner U | |mipnetlab=FR Grenoble Schlattner U | ||
}} | }} | ||
Latest revision as of 22:22, 17 October 2018
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Link: MitoEAGLE
Schlattner U (2018)
Event: MiPschool Tromso-Bergen 2018
Mitochondrial isoforms of nucleoside diphosphate kinase (NDPK-D or NME4) and creatine kinase (mtCK) are phylogenetically unrelated but share important structural and functional properties. They are both located in the intermembrane/cristae space and use mitochondrially generated ATP to phosphorylate their specific substrates, NDPs or creatine, thus regenerating ADP within the mitochondria. Both enzymes functionally interact with inner membrane adenylate translocator, thus allowing for privileged exchange (channeling) of these metabolites. We will discuss the molecular basis of this metabolite channeling and its functional consequences beyond the simple maintenance of proper nucleotide pools: stimulation of respiration, “energy export”, and regulation of ROS production, permeability transition, and mitochondrial shape.
• Bioblast editor: Beno M, Plangger M
• O2k-Network Lab: FR Grenoble Schlattner U
Affiliations
- Lab Fundamental Applied Bioenergetics SFR Environmental Systems Biology, Univ Grenoble Alpes Inserm, Grenoble, France
Labels: MiParea: Respiration
HRR: Oxygraph-2k Event: B1, Oral
