CATCHR, HOPS and CORVET tethering complexes share a similar architecture

Nat Struct Mol Biol. 2016 Aug;23(8):761-3. doi: 10.1038/nsmb.3264. Epub 2016 Jul 18.

Abstract

We show here that the Saccharomyces cerevisiae GARP complex and the Cog1-4 subcomplex of the COG complex, both members of the complexes associated with tethering containing helical rods (CATCHR) family of multisubunit tethering complexes, share the same subunit organization. We also show that HOPS, a tethering complex acting in the endolysosomal pathway, shares a similar architecture, thus suggesting that multisubunit tethering complexes use related structural frameworks.

MeSH terms

  • Adaptor Proteins, Vesicular Transport / ultrastructure
  • Membrane Transport Proteins / ultrastructure
  • Microscopy, Electron
  • Models, Molecular
  • Multiprotein Complexes / ultrastructure
  • Protein Structure, Quaternary
  • Protein Subunits / chemistry
  • Saccharomyces cerevisiae / ultrastructure*
  • Saccharomyces cerevisiae Proteins / ultrastructure
  • Vesicular Transport Proteins / ultrastructure

Substances

  • Adaptor Proteins, Vesicular Transport
  • COG2 protein, S cerevisiae
  • COG3 protein, S cerevisiae
  • COG4 protein, S cerevisiae
  • Cog1 protein, S cerevisiae
  • Membrane Transport Proteins
  • Multiprotein Complexes
  • Protein Subunits
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins