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A more recent version of this article appeared on February 27, 2004
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M313465200v1
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Papers In Press, published online ahead of print December 16, 2003
J. Biol. Chem, 10.1074/jbc.M313465200
Submitted on December 9, 2003
Revised on December 16, 2003
Accepted on December 16, 2003

WNK1 activates ERK5 by an MEKK2/3-dependent mechanism

Bing-e Xu, Steve Stippec, Lisa Lenertz, Byung-Hoon Lee, Wei Zhang, Youn-Kyoung Lee, and Melanie H. Cobb

Department of Pharmacology, University of Texas Southwestern, Dallas, TX 75390-9041

Corresponding Author: mcobb{at}mednet.swmed.edu

WNK1 belongs to a unique protein kinase family that lacks the catalytic lysine in its normal position. Mutations in human WNK1 and WNK4 have been implicated in causing a familial form of hypertension. Here we report that overexpression of WNK1 led to increased activity of cotransfected ERK5 in HEK293 cells. ERK5 activation was blocked by the MEK5 inhibitor U0126 and expression of a dominant-negative MEK5 mutant. Expression of dominant-negative mutants of MEKK2 and MEKK3 also blocked activation of ERK5 by WNK1. Moreover, both MEKK2 and MEKK3 coimmunoprecipitated with endogenous WNK1 from cell lysates. WNK1 phosphorylated both MEKK2 and 3 in vitro, and MEKK3 was activated by WNK1 in 293 cells. Finally, ERK5 activation by EGF was attenuated by suppression of WNK1 expression using siRNA. Taken together, these results place WNK1 in the ERK5 MAP kinase pathway upstream of MEKK2/3.


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