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Title: Phosphorylation of Src by phosphoinositide 3-kinase regulates beta-adrenergic receptor-mediated EGFR transactivation
Authors: Lewis J. Watson
Kevin M. Alexander
Maradumane L. Mohan
Amber L. Bowman
Supachoke Mangmool
Kunhong Xiao
Sathyamangla V. Naga Prasad
Howard A. Rockman
Duke University Medical Center
Cleveland Clinic Foundation
Mahidol University
University of Pittsburgh School of Medicine
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Oct-2016
Citation: Cellular Signalling. Vol.28, No.10 (2016), 1580-1592
Abstract: © 2016 Elsevier Inc. β2-Adrenergic receptors (β2AR) transactivate epidermal growth factor receptors (EGFR) through formation of a β2AR–EGFR complex that requires activation of Src to mediate signaling. Here, we show that both lipid and protein kinase activities of the bifunctional phosphoinositide 3-kinase (PI3K) enzyme are required for β2AR-stimulated EGFR transactivation. Mechanistically, the generation of phosphatidylinositol (3,4,5)-tris-phosphate (PIP3) by the lipid kinase function stabilizes β2AR–EGFR complexes while the protein kinase activity of PI3K regulates Src activation by direct phosphorylation. The protein kinase activity of PI3K phosphorylates serine residue 70 on Src to enhance its activity and induce EGFR transactivation following βAR stimulation. This newly identified function for PI3K, whereby Src is a substrate for the protein kinase activity of PI3K, is of importance since Src plays a key role in pathological and physiological signaling.
ISSN: 18733913
Appears in Collections:Scopus 2016-2017

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