Nature Communications (Mar 2017)

Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion

  • Christine Gundry,
  • Sergi Marco,
  • Elena Rainero,
  • Bryan Miller,
  • Emmanuel Dornier,
  • Louise Mitchell,
  • Patrick T. Caswell,
  • Andrew D. Campbell,
  • Anna Hogeweg,
  • Owen J. Sansom,
  • Jennifer P. Morton,
  • Jim C. Norman

DOI
https://doi.org/10.1038/ncomms14646
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 15

Abstract

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Ephrin receptors mediate contact inhibition, but their intracellular trafficking during this process is unknown. Here the authors show that EphA2 receptor trafficking is regulated by the Rab GTPase effector Rab-coupling protein, which associates with Rab14-endosomes upon LMTK3-mediated phosphorylation.