Phosphorylation or Mutation of the ERK2 Activation Loop Alters Oligonucleotide Binding.

ABSTRACT: The mitogen-activated protein kinase ERK2 is able to elicit a wide range of context-specific responses to distinct stimuli, but the mechanisms underlying this versatility remain in question. Some cellular functions of ERK2 are mediated through regulation of gene expression. In addition to phosphorylating numerous transcriptional regulators, ERK2 is known to associate with chromatin and has been shown to bind oligonucleotides directly. ERK2 is activated by the upstream kinases MEK1/2, which phosphorylate both tyrosine 185 and threonine 183. ERK2 requires phosphorylation on both sites to be fully active. Some additional ERK2 phosphorylation sites have also been reported, including threonine 188. It has been suggested that this phospho form has distinct properties. We detected some ERK2 phosp

SUBMITTER: McReynolds AC 

PROVIDER: S-EPMC5167559 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature