Related Experiment Video

Updated: Feb 15, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.5K

De-RSKing ERK - regulation of ERK1/2-RSK dissociation by phosphorylation within a disordered motif

Andrew M Kidger1, Simon J Cook1

  • 1Signalling Programme, The Babraham Institute, Cambridge, UK.

The FEBS Journal
|January 10, 2018
PubMed

Insights

Extracellular signal-regulated kinases (ERK1/2) and ribosomal S6 kinases (RSK) separate after ERK1/2 phosphorylates RSK. This phosphorylation creates a charge clamp, enabling both kinases to target other substrates.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Protein kinases ERK1/2 and RSK form complexes in unstimulated cells.
  • Dissociation of ERK1/2 and RSK is necessary for them to interact with other cellular targets.

Purpose of the Study:

  • To elucidate the mechanism by which ERK1/2 and RSK dissociate.
  • To understand the role of RSK phosphorylation in regulating kinase interactions.

Main Methods:

  • The study likely involved biochemical assays and structural analyses to investigate protein-protein interactions.
  • Phosphorylation site mapping and mutational analysis were probably employed.

Main Results:

  • Phosphorylation of RSK by active ERK1/2 induces an intramolecular charge clamp.
  • This clamp forms between Lys729 and the phosphate on Ser732 of RSK.
  • The charge clamp facilitates the dissociation of ERK1/2 from RSK.

Conclusions:

  • The findings reveal a novel regulatory mechanism for kinase dissociation.
  • This mechanism allows ERK1/2 and RSK to independently target diverse substrates.
  • Understanding this dissociation is key to comprehending complex cell signaling pathways.

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