Work

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

Year: 2009

Type: article

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.

Source: Molecular and Cellular Biology

DOI: 10.1128/mcb.00916-08

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

Institutions: Duke University, Duke Medical Center, University of North Carolina at Chapel Hill, UNC Lineberger Comprehensive Cancer Center

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: U.S. Department of Defense, National Institutes of Health, National Cancer Institute

Awards: G1992624342, Protein prenylation, oncogenesis and novel therapeutics, G250545864, G2545424317, G2978045611, Biological Activity of Ras Oncogenes, G3549828030, G5028106406, Developing inhibitors of RalA function for the treatment of pancreatic cancer, Inhibitors of Rho function as novel cancer therapeutics, G6776848823, RalA signal transduction, G9000329203, G9000341580

OpenAlex ID: W2100469448

FWCI: 4.625

Cites: 69

Cited by: 125

Related to: 10