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Papers In Press, published online ahead of print October 20, 2000
J. Biol. Chem, 10.1074/jbc.M005953200
Submitted on July 6, 2000
Revised on October 20, 2000
Accepted on October 20, 2000

p38 KINASE-DEPENDENT MAPKAPK-2 ACTIVATION FUNCTIONS AS PDK2 FOR AKT IN HUMAN NEUTROPHILS

Madhavi J. Rane, Patricia Y. Coxon, David W. Powell, Rose Webster, Jon B. Klein, Peipei Ping, William Pierce, and Kenneth R. McLeish

Medicine, University of Louisville, Louisville, KY 40202

Corresponding Author: mrane{at}louisville.edu

SUMMARY Akt activation requires phosphorylation of T308 and S473 by PDK1 and PDK2, respectively. While PDK1 has been cloned and sequenced, PDK2 has yet to be identified. The present study shows that PI-3K-dependent p38 kinase activation regulates Akt phosphorylation and activity in human neutrophils. Inhibition of p38 kinase activity with SB203580 inhibited Akt S473 phosphorylation following neutrophil stimulation with fMLP, FcgR crosslinking, or PIP3. Concentration inhibition studies showed S473 phosphorylation was inhibited by 0.3 mM SB203580, while inhibition of T308 phosphorylation required 10 mM 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 GST pull-down with GST-Akt or GST-MK2 showed that Akt was associated with p38 kinase, MK2, and Hsp27 in neutrophils, and Hsp27 dissociated from the complex upon fMLP stimulation. 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.


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