Apr 7, 2020 · In order to design a cardio-safe ERK1/2 inhibitor with new or extended indications, we here establish a molecular strategy that acts at the nucleocytosolic interface of ERK1/2 by interference with...

Sep 5, 2008 · Here we demonstrate that scaffolds and ERK dimers are essential for the activation of cytoplasmic but not nuclear substrates. Dimerization is critical for connecting the scaffolded ERK complex to cognate cytoplasmic substrates. Contrarily, nuclear substrates associate to …

Sep 5, 2008 · Here we demonstrate that scaffolds and ERK dimers are essential for the activation of cytoplasmic but not nuclear substrates. Dimerization is critical for connecting the scaffolded ERK complex to cognate cytoplasmic substrates. Contrarily, nuclear substrates associate to …

Jun 23, 2020 · By phosphorylating widely diverse substrates, ERK proteins govern a variety of evolutionarily conserved cellular processes in metazoans, the dysregulation of which contributes to the cause of...

Sep 5, 2008 · Here we demonstrate that scaffolds and ERK dimers are essential for the activation of cytoplasmic but not nuclear substrates. Dimerization is critical for connecting the scaffolded ERK complex to cognate cytoplasmic substrates. Contrarily, nuclear substrates associate to …

Extracellular signal-regulated kinase 1 (ERK1) and ERK2 are members of the mitogen-activated protein kinase (MAPK) family of serine/threonine kinases. They are activated in response to many stimuli, including those leading to cellular proliferation.

Two ERK monomers can associate to form a free dimer in the cytoplasm to activate cytoplasmic substrates. ERK dimers can be assembled on scaffold proteins in specific subcellular localizations where the ERK monomer not associated with the scaffold will …

Apr 4, 2012 · In this review, we summarize the various in vitro and in vivo studies concerning the Monomeric or the dimeric forms of ERK2 and the validity of the dimer hypothesis. Sustaining healthy individual cells is vital to the survival of a multicellular organism.

Dec 12, 2005 · Dimerisation of human recombinant ERK1 in vitro requires both ERK1 phosphorylation and cellular cofactor (s); it leads to the formation of a high molecular weight complex that can be dissociated by treatment with β-mercaptoethanol.

Here we demonstrate that scaffolds and ERK dimers are essential for the activation of cytoplasmic but not nuclear substrates. Dimerization is critical for connecting the scaffolded ERK complex to cognate cytoplasmic substrates. Contrarily, nuclear …