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Acetylation of cyclin-dependent kinase 5 is mediated by GCN5

Juhyung Lee1, Nuri Yun1, Chiho Kim1

  • 1Department of Systems Biology, Yonsei University College of Life Science and Biotechnology, Seoul 120-749, Republic of Korea.

Biochemical and Biophysical Research Communications
|April 8, 2014
PubMed

Insights

Acetylation is a newly discovered posttranslational modification for cyclin-dependent kinase 5 (CDK5). GCN5 enhances CDK5 acetylation at Lys33, potentially impacting kinase activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Cyclin-dependent kinase 5 (CDK5) is vital in neurodegenerative disease.
  • CDK5 activity is regulated by phosphorylation, S-nitrosylation, and activator binding.

Purpose of the Study:

  • To investigate acetylation as a novel posttranslational modification of CDK5.
  • To identify enzymes regulating CDK5 acetylation.

Main Methods:

  • Co-immunoprecipitation assays to confirm protein interactions.
  • Fluorescent localization studies for subcellular co-localization.
  • Liquid chromatography-mass spectrometry for identifying acetylation sites.

Main Results:

  • Acetylation enhances CDK5 modification within cells.
  • GCN5, a histone acetyltransferase, interacts with and enhances CDK5 acetylation.
  • CDK5 is acetylated at Lys33 in the ATP binding domain.
  • Lys33 is conserved across species and related kinases.

Conclusions:

  • Acetylation represents a new regulatory mechanism for CDK5.
  • GCN5-mediated acetylation of CDK5 at Lys33 may modulate its kinase activity by affecting ATP binding.
Keywords:
ATPAcetylationCDK5GCN5K33

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