TY - JOUR
T1 - Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact
AU - Shai, Nadav
AU - Yifrach, Eden
AU - van Roermund, Carlo W. T.
AU - Cohen, Nir
AU - Bibi, Chen
AU - Ijlst, Lodewijk
AU - Cavellini, Laetitia
AU - Meurisse, Julie
AU - Schuster, Ramona
AU - Zada, Lior
AU - Mari, Muriel C.
AU - Reggiori, Fulvio M.
AU - Hughes, Adam L.
AU - Escobar-Henriques, Mafalda
AU - Cohen, Mickael M.
AU - Waterham, Hans R.
AU - Wanders, Ronald J. A.
AU - Schuldiner, Maya
AU - Zalckvar, Einat
PY - 2018
Y1 - 2018
N2 - 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.
AB - 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.
UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85046474245&origin=inward
UR - https://www.ncbi.nlm.nih.gov/pubmed/29720625
U2 - https://doi.org/10.1038/s41467-018-03957-8
DO - https://doi.org/10.1038/s41467-018-03957-8
M3 - Article
C2 - 29720625
SN - 2041-1723
VL - 9
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 1761
ER -