Aurora-A Phosphorylates, Activates, and Relocalizes the Small GTPase RalA | Zendy

KianHuat Lim | Zendy; Donita C. Brady | Zendy; David F. Kashatus | Zendy; Brooke B. Ancrile | Zendy; Channing J. Der | Zendy; Adrienne D. Cox | Zendy; Christopher M. Counter | Zendy

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Aurora-A Phosphorylates, Activates, and Relocalizes the Small GTPase RalA

Author(s) -

KianHuat Lim,

Donita C. Brady,

David F. Kashatus,

Brooke B. Ancrile,

Channing J. Der,

Adrienne D. Cox,

Christopher M. Counter

Publication year - 2009

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.00916-08

Subject(s) - biology , small gtpase , microbiology and biotechnology , gtpase , mitosis , phosphorylation , gtpase activating protein , effector , signal transduction , cancer research , g protein

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.

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