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Identification of Transcription Factor Regulators using Medium-Throughput Screening of Arrayed Libraries and a Dual-Luciferase-Based Reporter
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Modulation of Krüppel-like factors (KLFs) interaction with their binding partners in cancers through acetylation and

Kanupriya Jha1, Amit Kumar1, Kartik Bhatnagar1

  • 1Department of Biotechnology, School of Engineering and Applied Sciences, Bennett University, Plot Nos. 8-11, Tech Zone 2, Greater Noida, Uttar Pradesh 201310, India.

Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms
|November 22, 2023
PubMed

Insights

Post-translational modifications (PTMs) like acetylation and phosphorylation act as molecular switches for Krüppel-like transcription factors (KLFs). These modifications influence KLF interactions, explaining their dual role in cancer suppression or activation.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Biology

Background:

  • Post-translational modifications (PTMs) are crucial for regulating protein function and increasing proteome complexity.
  • Krüppel-like transcription factors (KLFs) are key regulators of cellular processes, including proliferation, differentiation, and cancer development.
  • The dual role of KLF group-2 members as cancer suppressors or activators is often observed but lacks molecular explanation.

Purpose of the Study:

  • To investigate the impact of acetylation and phosphorylation on the binding affinity of KLF group-2 members with their partners.
  • To elucidate the molecular mechanisms underlying the context-dependent functions of KLFs in cancer.

Main Methods:

  • The study focused on analyzing the interactions between KLF group-2 members and their known binding partners.
  • Specific PTMs (acetylation and phosphorylation) at various positions within KLFs were assessed for their effects on binding interactions.

Main Results:

  • Acetylation and phosphorylation at different sites on KLFs exhibited variable effects on their binding affinities with specific partners.
  • Some KLF-partner interactions, such as KLF2-EP300 and KLF6-JUN, were stabilized by these modifications.
  • Other interactions, including KLF4-CBP and KLF5-WWP1, showed either stabilization or destabilization depending on the specific PTM and its position.

Conclusions:

  • PTMs significantly modulate KLF group-2 member interactions with their binding partners.
  • These PTM-dependent changes in binding affinity provide a molecular basis for the observed dual role of KLFs in cancer.
  • Understanding these modifications is essential for deciphering KLF functions in both normal biological processes and disease states.
Keywords:
AcetylationCancerKrüppel-like transcription factors (KLFs)PhosphorylationPost-translational modification (PTM)

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