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Updated: Jan 25, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

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Cyclin-Dependent Kinase 5 (CDK5)-Mediated Phosphorylation of Upstream Stimulatory Factor 2 (USF2) Contributes to

Tabughang Franklin Chi1, Tina Horbach2, Claudia Götz3

  • 1Faculty of Biochemistry and Molecular Medicine, University of Oulu, 90014 Oulu, Finland. Franklin.Tabughang@oulu.fi.

Cancers
|April 25, 2019
PubMed

Insights

Cyclin-dependent kinase 5 (CDK5) phosphorylates the transcription factor USF2, stabilizing it and influencing cancer cell growth and migration. This CDK5-USF2 interaction is crucial in tumor development.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cellular Signaling

Background:

  • The transcription factor USF2 plays a role in tumor development.
  • Regulatory mechanisms of USF2 are largely unknown.
  • High CDK5 and USF2 expression correlate with various cancers.

Purpose of the Study:

  • To investigate the regulatory mechanisms of USF2.
  • To identify the relationship between CDK5 and USF2 in cancer.

Main Methods:

  • Phosphorylation assays to identify USF2 as a CDK5 target.
  • Site-directed mutagenesis to pinpoint phosphorylation sites.
  • Analysis of protein stability, cellular growth, and migration.

Main Results:

  • USF2 is a direct phosphorylation target of CDK5.
  • CDK5 phosphorylates USF2 at serine 155 and serine 222.
  • Phosphorylation stabilizes USF2 and regulates cancer cell growth and migration.

Conclusions:

  • The CDK5-USF2 interaction is a key regulatory mechanism in cancer.
  • CDK5-mediated USF2 phosphorylation influences tumor progression.
  • Targeting the CDK5-USF2 pathway may offer therapeutic strategies.
Keywords:
CRISPR-Cas9cyclin-dependent kinase-5 (CDK5)migrationphosphorylationproliferationupstream stimulatory factor 2 (USF2)

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