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Transforming growth factor-β-inducible early response gene 1 is a novel substrate for atypical protein kinase Cs

Endalkachew A Alemu1, Eva Sjøttem, Heidi Outzen

  • 1Molecular Cancer Research Group, Institute of Medical Biology, University of Tromsö, Tromsö 9037, Norway.

Cellular and Molecular Life Sciences : CMLS
|October 19, 2010
PubMed

Insights

Atypical protein kinase Cs (aPKCs) interact with and phosphorylate the TIEG1 protein. This phosphorylation impacts TIEG1

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein kinase C (PKC) family comprises ten isoforms in three subfamilies: classical, novel, and atypical (aPKCs).
  • Atypical PKCs, specifically PKCι/λ and PKCζ, are crucial for developmental processes and cancer-related functions like cell polarity, proliferation, differentiation, and apoptosis.

Purpose of the Study:

  • To identify novel interaction partners for atypical PKCs (aPKCs).
  • To investigate the functional consequences of aPKC interaction with identified partners.

Main Methods:

  • Yeast two-hybrid screen using the regulatory domain of PKCι/λ as bait.
  • In vitro and in-cell interaction confirmation assays.
  • Analysis of TIEG1 phosphorylation, DNA-binding activity, subnuclear localization, and transactivation potential.

Main Results:

  • The Krüppel-like factor protein TIEG1 was identified as a putative interaction partner for PKCι/λ.
  • Both aPKCs (PKCι/λ and PKCζ) interact with TIEG1.
  • aPKCs phosphorylate TIEG1 within its DNA-binding domain at two critical residues.
  • Phosphorylation of TIEG1 by aPKCs alters its DNA-binding activity, subnuclear localization, and transactivation potential.

Conclusions:

  • TIEG1 is a novel interaction partner for atypical PKCs.
  • aPKC-mediated phosphorylation regulates TIEG1 function, impacting its role in gene regulation.
  • These findings provide new insights into the regulatory mechanisms of aPKCs and TIEG1 in cellular processes.

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