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Related Experiment Videos

Phosphorylation negatively regulates the function of coactivator PC4

H Ge1, Y Zhao, B T Chait

  • 1Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.

Proceedings of the National Academy of Sciences of the United States of America
|December 20, 1994
PubMed
Summary

Human positive cofactor 4 (PC4) is essential for gene transcription. In vivo phosphorylation by casein kinase II inactivates PC4, revealing a novel regulatory mechanism for transcriptional cofactors.

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein Biochemistry

Background:

  • Human positive cofactor 4 (PC4) is a key mediator of activator-dependent transcription by RNA polymerase II.
  • PC4 interacts with transcriptional activators and the basal transcription machinery to regulate gene expression.

Purpose of the Study:

  • To investigate the role of in vivo phosphorylation in modulating the function of human positive cofactor 4 (PC4).
  • To identify the specific kinases involved in PC4 phosphorylation and the functional consequences of this modification.

Main Methods:

  • Protein-protein interaction studies
  • In vitro transcription assays
  • Mutational analysis
  • Mass spectrometry

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Main Results:

  • Only the nonphosphorylated form of PC4 is functionally active in transcription.
  • In vivo hyperphosphorylation of PC4 is primarily mediated by casein kinase II.
  • Phosphorylation is restricted to an N-terminal serine-rich region of PC4.

Conclusions:

  • PC4 function is negatively regulated by casein kinase II-mediated phosphorylation.
  • This study provides an example of a transcriptional cofactor regulated by phosphorylation, impacting gene transcription.