CK2 phosphorylates TNFAIP1 to affect its subcellular localization and interaction with PCNA

Mol Biol Rep. 2010 Jul;37(6):2967-73. doi: 10.1007/s11033-009-9863-1. Epub 2009 Oct 23.

Abstract

TNFAIP1 is a protein which can be induced by tumor necrosis factoralpha (TNFalpha) and interleukin-6 (IL-6), it may play roles in DNA synthesis, DNA repair, cell apoptosis and human diseases. However, very little has been known about how TNFAIP1 acts in these physiological processes. In this paper, CK2beta was identified as a partner of TNFAIP1 by screening the HeLa cDNA library in yeast two-hybrid system with TNFAIP1 as a bait. Furthermore, it was demonstrated that CK2 could phosphorylate TNFAIP1 in vitro and in vivo, which facilitated the distribution of TNFAIP1 in nucleus and enhanced its interaction with PCNA. It is suggested that the phosphorylation of TNFAIP1 may be required for its functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Casein Kinase II / metabolism*
  • Cell Nucleus / metabolism
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Phosphorylation
  • Phosphoserine / metabolism
  • Proliferating Cell Nuclear Antigen / metabolism*
  • Protein Binding
  • Protein Transport
  • Proteins / chemistry
  • Proteins / metabolism*
  • Subcellular Fractions / metabolism
  • Two-Hybrid System Techniques

Substances

  • Adaptor Proteins, Signal Transducing
  • Proliferating Cell Nuclear Antigen
  • Proteins
  • TNFAIP1 protein, human
  • Phosphoserine
  • Casein Kinase II