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Related Experiment Videos

CCAAT/enhancer binding protein epsilon: changes in function upon phosphorylation by p38 MAP kinase.

Elizabeth A Williamson1, Ian K Williamson, Alexey M Chumakov

  • 1Department of Medicine, Hematology/Oncology, Cedars-Sinai Medical Center, University of California-Los Angeles, USA. ewilliamson@salud.unm.edu

Blood
|January 29, 2005
PubMed
Summary

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CCAAT/enhancer binding protein epsilon (C/EBPepsilon) is phosphorylated by p38 MAP kinase at threonine 75. This phosphorylation enhances C/EBPepsilon

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Transcription Factors

Background:

  • C/EBPepsilon is a key transcription factor in neutrophil differentiation.
  • Post-translational modifications, including phosphorylation, regulate C/EBPepsilon activity.
  • Mitogen-activated protein (MAP) kinases are critical signaling enzymes involved in cellular responses.

Purpose of the Study:

  • To investigate the phosphorylation sites of C/EBPepsilon.
  • To identify the specific kinases that phosphorylate C/EBPepsilon.
  • To determine the functional consequences of C/EBPepsilon phosphorylation by p38 MAP kinase.

Main Methods:

  • Mass spectrometry to identify phosphorylation sites.
  • In vitro kinase assays using various kinases.

Related Experiment Videos

  • Transient transfection reporter assays to assess transcriptional activity.
  • Electrophoretic mobility shift assays (EMSAs) to evaluate DNA binding.
  • Stable cell line expression (32Dcl3) to study gene expression.

    • Main Results:

    • C/EBPepsilon is phosphorylated on multiple serine and threonine residues.
    • Threonine 75 (Thr75) within the transactivation domain is specifically phosphorylated by p38 MAP kinase.
    • Phosphorylation at Thr75 enhances C/EBPepsilon's transcriptional activity on myeloid-specific promoters.
    • Phosphorylation at Thr75 increases the DNA-binding affinity of C/EBPepsilon.
    • Mutating Thr75 to alanine (T75A) or aspartate (T75D) abrogated the expected functional outcomes observed with wild-type C/EBPepsilon.

    Conclusions:

    • C/EBPepsilon is a direct target of p38 MAP kinase.
    • Phosphorylation of C/EBPepsilon at Thr75 by p38 MAP kinase is a critical regulatory mechanism.
    • This phosphorylation event enhances C/EBPepsilon's function in transcriptional regulation and DNA binding, impacting neutrophil differentiation pathways.