Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

Nat Commun. 2018 May 2;9(1):1761. doi: 10.1038/s41467-018-03957-8.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cytoplasm / metabolism
  • GTP Phosphohydrolases / metabolism
  • Intracellular Membranes / metabolism*
  • Membrane Proteins / metabolism
  • Mitochondria / metabolism*
  • Mitochondrial Proteins / metabolism
  • Peroxins / metabolism
  • Peroxisomes / metabolism*
  • Protein Binding
  • Protein Interaction Mapping
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism


  • Membrane Proteins
  • Mitochondrial Proteins
  • Peroxins
  • Pex34 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • FZO1 protein, S cerevisiae
  • GTP Phosphohydrolases