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Updated: Aug 6, 2026

Temporal Quantification of MAPK Induced Expression in Single Yeast Cells
07:59

Temporal Quantification of MAPK Induced Expression in Single Yeast Cells

Published on: October 4, 2013

Expression and characterization of MAP kinases in bacteria

Charles J Heise1, Melanie H Cobb

  • 1Department of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park Road, Dallas, TX 75390-9041, USA.

Methods (San Diego, Calif.)
|August 16, 2006
PubMed

Insights

Mitogen-activated protein kinases (MAPKs) are crucial in eukaryotic cell signaling. This study details methods to phosphorylate or thiophosphorylate ERK2 in vitro, aiding MAPK network research.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitogen-activated protein kinases (MAPKs) are essential signal transducers in eukaryotes.
  • MAPKs, including Extracellular-signal regulated kinases 1 and 2 (ERK1/2), are activated via kinase cascades (MAP3Ks, MAP2Ks).
  • MAPK activity is tightly regulated by phosphorylation and dephosphorylation.

Purpose of the Study:

  • To describe a method for in vitro phosphorylation and thiophosphorylation of ERK2.
  • To provide a tool for investigating mitogen-activated protein kinase signaling pathways.

Main Methods:

  • In vitro phosphorylation of ERK2.
  • In vitro thiophosphorylation of ERK2.

Main Results:

  • Successful phosphorylation of ERK2 in vitro.
  • Successful thiophosphorylation of ERK2 in vitro.

Conclusions:

  • The described in vitro phosphorylation and thiophosphorylation methods are valuable for studying MAPK signaling.
  • These techniques enable further investigation into the complex MAPK signaling networks.

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