Aurora-A phosphorylates, activates, and relocalizes the small GTPase RalA

Mol Cell Biol. 2010 Jan;30(2):508-23. doi: 10.1128/MCB.00916-08. Epub 2009 Nov 9.

Abstract

The small GTPase Ras, which transmits extracellular signals to the cell, and the kinase Aurora-A, which promotes proper mitosis, can both be inappropriately activated in human tumors. Here, we show that Aurora-A in conjunction with oncogenic Ras enhances transformed cell growth. Furthermore, such transformation and in some cases also tumorigenesis depend upon S194 of RalA, a known Aurora-A phosphorylation site. Aurora-A promotes not only RalA activation but also translocation from the plasma membrane and activation of the effector protein RalBP1. Taken together, these data suggest that Aurora-A may converge upon oncogenic Ras signaling through RalA.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism*
  • Animals
  • Aurora Kinase A
  • Aurora Kinases
  • Cell Line, Tumor
  • GTPase-Activating Proteins / genetics
  • GTPase-Activating Proteins / metabolism*
  • Humans
  • Mice
  • Mice, SCID
  • Mutation
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Xenograft Model Antitumor Assays
  • ral GTP-Binding Proteins / genetics
  • ral GTP-Binding Proteins / metabolism*
  • ras Proteins / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • GTPase-Activating Proteins
  • RALBP1 protein, human
  • Aurka protein, mouse
  • Aurora Kinase A
  • Aurora Kinases
  • Protein Serine-Threonine Kinases
  • RALA protein, human
  • ral GTP-Binding Proteins
  • ras Proteins