A5011042714- Mitochondrial Function and Pathology
- ATP Synthase and ATPases Research
- Endoplasmic Reticulum Stress and Disease
- Metabolism and Genetic Disorders
- Ubiquitin and proteasome pathways
- Heat shock proteins research
- Photosynthetic Processes and Mechanisms
- RNA and protein synthesis mechanisms
- Autophagy in Disease and Therapy
- Adipose Tissue and Metabolism
- Enzyme Structure and Function
- RNA modifications and cancer
- Genetic Neurodegenerative Diseases
- Protein Structure and Dynamics
- Neurological diseases and metabolism
- Lipid metabolism and biosynthesis
- Hereditary Neurological Disorders
- Signaling Pathways in Disease
- thermodynamics and calorimetric analyses
- Urinary Tract Infections Management
- Peptidase Inhibition and Analysis
- interferon and immune responses
- RNA Research and Splicing
- Cancer, Hypoxia, and Metabolism
- Microtubule and mitosis dynamics
Max Planck Institute for Biology of Ageing
2015-2025
University of Cologne
2015-2024
Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases
2015-2024
University of Milano-Bicocca
2024
German Cancer Society
2024
Azienda Socio Sanitaria Territoriale Grande Ospedale Metropolitano Niguarda
2024
Max Planck Society
2012-2019
Institute of Genetics
2009-2016
Institute for Molecular Medicine
2014
National Institutes of Health
2013
Mitochondrial fusion and structure depend on the dynamin-like GTPase OPA1, whose activity is regulated by proteolytic processing. Constitutive OPA1 cleavage YME1L OMA1 at two distinct sites leads to accumulation of both long short forms maintains mitochondrial fusion. Stress-induced processing converts completely into isoforms, inhibits fusion, triggers fragmentation. Here, we have analyzed function different in cells lacking YME1L, OMA1, or both. Unexpectedly, deletion Oma1 restored...
Mitochondrial fusion depends on the dynamin-like guanosine triphosphatase OPA1, whose activity is controlled by proteolytic cleavage. Dysfunction of mitochondria induces OPA1 processing and results in mitochondrial fragmentation, allowing selective removal damaged mitochondria. In this study, we demonstrate that two classes metallopeptidases regulate cleavage inner membrane: isoenzymes adenosine triphosphate (ATP)-dependent matrix AAA (ATPase associated with diverse cellular activities...
Prohibitins comprise an evolutionarily conserved and ubiquitously expressed family of membrane proteins with poorly described functions. Large assemblies PHB1 PHB2 subunits are localized in the inner mitochondria, but various roles other cellular compartments have also been proposed for both proteins. Here, we used conditional gene targeting murine Phb2 to define activities prohibitins. Our experiments restrict function prohibitins mitochondria identify processing dynamin-like GTPase OPA1,...
Prohibitin ring complexes in the mitochondrial inner membrane regulate cell proliferation as well dynamics and function of mitochondria. Although prohibitins are essential higher eukaryotes, prohibitin-deficient yeast cells viable exhibit a reduced replicative life span. Here, we define genetic interactome using synthetic arrays, identify 35 interactors (GEP genes) required for survival absence prohibitins. Proteins encoded by these genes include members conserved protein family, Ups1 Gep1,...
Mitochondria are dynamic organelles whose function depends on intramitochondrial phospholipid synthesis and the supply of membrane lipids from endoplasmic reticulum. How phospholipids transported to in-between mitochondrial membranes remained unclear. We identified Ups1, a yeast member conserved family intermembrane space proteins, as lipid transfer protein that can shuttle phosphatidic acid between membranes. Lipid required assembly Ups1 with Mdm35 allowed conversion cardiolipin in inner...