Article
An analysis of the phosphorylation and activation of extracellular-signal-regulated protein kinase 5 (ERK5) by mitogen-activated protein kinase kinase 5 (MKK5) in vitro.
The Biochemical journal - 1 Jun 2003
Mody Nimesh, Campbell David G, Morrice Nick, Peggie Mark, Cohen Philip
Abstract excerpt
MKK5 expressed as a glutathione S-transferase fusion protein in human embryonic kidney 293 cells activated full-length extracellular-signal-regulated protein kinase (ERK)5 (ERK5wt) as well as the isolated catalytic domain (ERK5cat) in vitro. Activation was accompanied by the phosphorylation of Thr(219) and Tyr(221), the former residue being phosphorylated preferentially. ERK5cat phosphorylated at Thr(219), but...
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