Aurora-A phosphorylates, activates, and relocalizes the small GTPase Ra1A

  • Kian Huat Lim
  • , Donita C. Brady
  • , David F. Kashatus
  • , Brooke B. Ancrile
  • , Channing J. Der
  • , Adrienne D. Cox
  • , Christopher M. Counter

Research output: Contribution to journalArticlepeer-review

107 Scopus citations

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.

Original languageEnglish
Pages (from-to)508-523
Number of pages16
JournalMolecular and cellular biology
Volume30
Issue number2
DOIs
StatePublished - Jan 2010

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