Receptor association and tyrosine phosphorylation of S6 kinases

The FEBS Journal
Heike RebholzIvan T Gout

Abstract

Ribosomal protein S6 kinase (S6K) is activated by an array of mitogenic stimuli and is a key player in the regulation of cell growth. The activation process of S6 kinase involves a complex and sequential series of multiple Ser/Thr phosphorylations and is mainly mediated via phosphatidylinositol 3-kinase (PI3K)-3-phosphoinositide-dependent protein kinase-1 (PDK1) and mTor-dependent pathways. Upstream regulators of S6K, such as PDK1 and protein kinase B (PKB/Akt), are recruited to the membrane via their pleckstrin homology (PH) or protein-protein interaction domains. However, the mechanism of integration of S6K into a multi-enzyme complex around activated receptor tyrosine kinases is not clear. In the present study, we describe a specific interaction between S6K with receptor tyrosine kinases, such as platelet-derived growth factor receptor (PDGFR). The interaction with PDGFR is mediated via the kinase or the kinase extension domain of S6K. Complex formation is inducible by growth factors and leads to S6K tyrosine phosphorylation. Using PDGFR mutants, we have shown that the phosphorylation is exerted via a PDGFR-src pathway. Furthermore, src kinase phosphorylates and coimmunoprecipitates with S6K in vivo. Inhibitors towards tyros...Continue Reading

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Citations

May 22, 2008·American Journal of Physiology. Endocrinology and Metabolism·Can PangJianping Ye
Jul 14, 2006·BMC Bioinformatics·Cheryl WoltingDavid Tritchler
May 9, 2012·Expert Opinion on Therapeutic Targets·Carman K M Ip, Alice S T Wong
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Feb 15, 2020·International Journal of Molecular Sciences·Savitha Sridharan, Alakananda Basu
May 12, 2021·Cellular Signalling·Lilas AlboushiSeyed Mehdi Jafarnejad

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