Ontology highlight
ABSTRACT:
SUBMITTER: Perander M
PROVIDER: S-EPMC5333157 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Perander Maria M Al-Mahdi Rania R Jensen Thomas C TC Nunn Jennifer A L JA Kildalsen Hanne H Johansen Bjarne B Gabrielsen Mads M Keyse Stephen M SM Seternes Ole-Morten OM
Scientific reports 20170302
The atypical MAP kinases ERK3 and ERK4 are activated by phosphorylation of a serine residue lying within the activation loop signature sequence S-E-G. However, the regulation of ERK3 and ERK4 phosphorylation and activity is poorly understood. Here we report that the inducible nuclear dual-specificity MAP kinase phosphatase (MKP) DUSP2, a known regulator of the ERK and p38 MAPKs, is unique amongst the MKP family in being able to bind to both ERK3 and ERK4. This interaction is mediated by a conser ...[more]