Nature Communications (Nov 2017)

Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5

  • Kevin Bärlocher,
  • Cedric A. J. Hutter,
  • A. Leoni Swart,
  • Bernhard Steiner,
  • Amanda Welin,
  • Michael Hohl,
  • François Letourneur,
  • Markus A. Seeger,
  • Hubert Hilbi

DOI
https://doi.org/10.1038/s41467-017-01512-5
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 15

Abstract

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Legionella pneumophila replicates in a Legionella-containing vacuole (LCV). Here the authors present the structure of the Legionella effector RidL N-terminal domain and reveal how RidL contributes to the subversion of retrograde trafficking by binding to the retromer coat complex subunit Vps29, which leads to a displacement of the regulator TBC1D5.