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Related Experiment Videos

Multiple and cooperative phosphorylation events regulate the CREM activator function

R P de Groot1, J den Hertog, J R Vandenheede

  • 1Laboratoire Génétique Moléculaire des Eucaryotes, CNRS, U184 de l'INSERM, Faculté de Médecine, Institut de Chimie Biologique, Strasbourg, France.

The EMBO Journal
|October 1, 1993
PubMed
Summary
This summary is machine-generated.

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Phosphorylation regulates the transcription factor CREM tau activity. Multiple phosphorylation events, especially on serine 117, enhance CREM tau

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Gene Regulation

Background:

  • Transcription factor activity is often modulated by post-translational modifications.
  • Phosphorylation is a key regulatory mechanism for transcription factors.

Purpose of the Study:

  • To investigate the role of phosphorylation in regulating the transcription factor CREM (cAMP response element modulator).
  • To identify specific phosphorylation sites and kinases involved in CREM tau regulation.

Main Methods:

  • In vivo and in vitro phosphorylation assays.
  • Analysis of CREM tau phosphorylation upon stimulation of signal transduction pathways (forskolin, TPA, Ca2+ ionophore).
  • Kinase identification and characterization.

Main Results:

Related Experiment Videos

  • CREM tau is phosphorylated on multiple serine and threonine residues in vivo.
  • Stimulation enhances phosphorylation of serine 117, increasing CREM tau's transactivation potential.
  • Casein kinases I and II cooperatively phosphorylate CREM tau, enhancing DNA binding.

Conclusions:

  • CREM tau activity is controlled by multiple phosphorylation events.
  • CREM functions as a nuclear effector integrating various signaling pathways.