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An intrinsic ATPase activity of phospho-MEK-1 uncoupled from downstream ERK phosphorylation.

Abstract：

:We have developed a highly sensitive assay of MEK-mediated ATP hydrolysis by coupling the formation of ADP to NADH oxidation through the enzymes pyruvate kinase and lactate dehydrogenase. Robust ATP hydrolysis is catalyzed by phosphorylated MEK in the absence of the protein substrate ERK. This ERK-uncoupled ATPase activity is dependent on the phosphorylation status of MEK and is abrogated by the selective MEK kinase inhibitor U0126. ADP production is concomitant with Raf-mediated phosphorylation of MEK. Based on this finding, a coupled Raf/MEK assay is developed for measuring the Raf activity. A kinetic treatment derived under steady-state assumptions is presented for the analysis of the reaction progress curve generated by this coupled assay. We have shown that inhibitory potency of selective Raf inhibitors can be determined accurately by this assay.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Rominger CM,Schaber MD,Yang J,Gontarek RR,Weaver KL,Broderick T,Carter L,Copeland RA,May EW

doi

10.1016/j.abb.2007.04.004

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

130-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(07)00183-X

journal_volume

464

pub_type

杂志文章

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