Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact
Autor: | Julie Meurisse, Ramona Schuster, Chen Bibi, Lodewijk IJlst, Nadav Shai, Nir Cohen, Muriel Mari, Einat Zalckvar, Mafalda Escobar-Henriques, Hans R. Waterham, Adam Hughes, Laetitia Cavellini, Eden Yifrach, Mickael M. Cohen, Maya Schuldiner, Carlo W.T. van Roermund, Ronald J.A. Wanders, Lior Zada, Fulvio Reggiori |
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Přispěvatelé: | Weizmann Institute of Science [Rehovot, Israël], University of Amsterdam [Amsterdam] (UvA), Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes (LBMCE), Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), University of Cologne, University Medical Center Groningen [Groningen] (UMCG), University of Utah School of Medicine [Salt Lake City], Laboratory Genetic Metabolic Diseases, AGEM - Inborn errors of metabolism, APH - Methodology, Microbes in Health and Disease (MHD), Center for Liver, Digestive and Metabolic Diseases (CLDM) |
Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
Intracellular Membranes/metabolism
0301 basic medicine Cytoplasm General Physics and Astronomy [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] Mitochondrion GTP Phosphohydrolases Peroxins SACCHAROMYCES-CEREVISIAE Bimolecular fluorescence complementation PROTEIN-PROTEIN INTERACTIONS Saccharomyces cerevisiae/metabolism 0302 clinical medicine FUSION Protein Interaction Mapping lcsh:Science Multidisciplinary Chemistry Tethering High-throughput screening Peroxins/metabolism Peroxisome Saccharomyces cerevisiae Proteins/metabolism Cytoplasm/metabolism 3. Good health Mitochondria Systematic mapping Protein Binding Mitochondrial Proteins/metabolism Saccharomyces cerevisiae Proteins Science MITOFUSIN SIGNAL PEPTIDE PREDICTION Saccharomyces cerevisiae General Biochemistry Genetics and Molecular Biology Article Protein–protein interaction Mitochondrial Proteins 03 medical and health sciences Mitochondria/metabolism Peroxisomes YEAST LIBRARIES Organelles Binding Sites BIMOLECULAR FLUORESCENCE COMPLEMENTATION Peroxisomes/metabolism Membrane Proteins General Chemistry Intracellular Membranes COMBINED TRANSMEMBRANE TOPOLOGY 030104 developmental biology ER PLASMA-MEMBRANE Biophysics Proximity detection lcsh:Q Membrane Proteins/metabolism GTP Phosphohydrolases/metabolism 030217 neurology & neurosurgery Function (biology) |
Zdroj: | Nature Communications Nature Communications, Nature Publishing Group, 2018, 9, pp.1761. ⟨10.1038/s41467-018-03957-8⟩ Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018) Nature communications, 9(1):1761. Nature Publishing Group Shai, N, Yifrach, E, van Roermund, C W T, Cohen, N, Bibi, C, IJlst, L, Cavellini, L, Meurisse, J, Schuster, R, Zada, L, Mari, M C, Reggiori, F M, Hughes, A L, Escobar-Henriques, M, Cohen, M M, Waterham, H R, Wanders, R J A, Schuldiner, M & Zalckvar, E 2018, ' Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact ', Nature Communications, vol. 9, no. 1, pp. 1761 . https://doi.org/10.1038/s41467-018-03957-8 Nature Communications, 9(1):1761. Nature Publishing Group |
ISSN: | 2041-1723 |
DOI: | 10.1038/s41467-018-03957-8 |
Popis: | The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in β-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease. The internal organization of the cell has been enriched by the discovery that organelles establish membrane contact sites, however the entire repertoire of these contacts is still being explored. Here the authors systematically identify the landscape of cellular contact sites in yeast, discovering four potential novel contact sites and two tether proteins for the peroxisome-mitochondria contact site. |
Databáze: | OpenAIRE |
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