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Originally published In Press as doi:10.1074/jbc.M005953200 on October 20, 2000

J. Biol. Chem., Vol. 276, Issue 5, 3517-3523, February 2, 2001
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p38 Kinase-dependent MAPKAPK-2 Activation Functions as 3-Phosphoinositide-dependent Kinase-2 for Akt in Human Neutrophils*

Madhavi J. RaneDagger §, Patricia Y. CoxonDagger , Dave W. Powell, Rose WebsterDagger , Jon B. KleinDagger ||, William Pierce**, Peipei PingDagger Dagger Dagger , and Kenneth R. McLeishDagger ||

From the Departments of Dagger  Medicine,  Biochemistry and Molecular Biology, Dagger Dagger  Physiology and Biophysics, and ** Pharmacology and Toxicology, University of Louisville Health Sciences Center and the || Veterans Affairs Medical Center, Louisville, Kentucky 40202

Akt activation requires phosphorylation of Thr308 and Ser473 by 3-phosphoinositide-dependent kinase-1 and 2 (PDK1 and PDK2), respectively. While PDK1 has been cloned and sequenced, PDK2 has yet to be identified. The present study shows that phosphatidylinositol 3-kinase-dependent p38 kinase activation regulates Akt phosphorylation and activity in human neutrophils. Inhibition of p38 kinase activity with SB203580 inhibited Akt Ser473 phosphorylation following neutrophil stimulation with formyl-methionyl-leucyl-phenylalanine, Fcgamma R cross-linking, or phosphatidylinositol 3,4,5-trisphosphate. Concentration inhibition studies showed that Ser473 phosphorylation was inhibited by 0.3 µM SB203580, while inhibition of Thr308 phosphorylation required 10 µM SB203580. Transient transfection of HEK293 cells with adenoviruses containing constitutively active MKK3 or MKK6 resulted in activation of both p38 kinase and Akt. Immunoprecipitation and glutathione S-transferase (GST) pull-down studies showed that Akt was associated with p38 kinase, MK2, and Hsp27 in neutrophils, and Hsp27 dissociated from the complex upon activation. Active recombinant MK2 phosphorylated recombinant Akt and Akt in anti-Akt, anti-MK2, anti-p38, and anti-Hsp27 immunoprecipitates, and this was inhibited by an MK2 inhibitory peptide. We conclude that Akt exists in a signaling complex containing p38 kinase, MK2, and Hsp27 and that p38-dependent MK2 activation functions as PDK2 in human neutrophils.

* This work was supported by National Institutes of Health (NIH) Grant HL63901 (to P. P.) and grants from the American Heart Association (to M. J. R. and K. R. M.), the American Heart Association Kentucky Affiliate (to P. Y. C.), the Department of Veterans Affairs (to K. R. M and J. B. K.), and the Jewish Hospital Foundation (to K. R. M. and J. B. K.). The Biomolecular Mass Spectrometry Laboratory is supported in part by NIH Grant 1S10RR11368-01A1, the State of Kentucky Physical Facilities Trust Fund, the University of Louisville School of Medicine, and the University of Louisville Research Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Molecular Signaling Group, Kidney Disease Program, 615 S. Preston St., University of Louisville, Louisville, KY 40202-1718. Tel.: 502-852-1159; Fax: 502-852-4384; E-mail: mrane@louisville.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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