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
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