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Phosphorylation of Tat-interactive protein 60 kDa by protein kinase C epsilon is important for its subcellular localisation.

Tat-interactive protein 60 kDa is a nuclear acetyltransferase that both coactivates and corepresses transcription factors and has a definitive function in the DNA damage response. Here, we provide evidence that Tat-interactive protein 60 kDa is phosphorylated by protein kinase C epsilon. In vitro, protein kinase C epsilon phosphorylates Tat-interactive protein 60 kDa on at least two sites within the acetyltransferase domain. In whole cells, activation of protein kinase C increases the levels of phosphorylated Tat-interactive protein 60 kDa and the interaction of Tat-interactive protein 60 kDa with protein kinase C epsilon. A phosphomimetic mutant Tat-interactive protein 60 kDa has distinct subcellular localisation compared to the wild-type protein in whole cells. Taken together, these findings suggest that the protein kinase C epsilon phosphorylation sites on Tat-interactive protein 60 kDa are important for its subcellular localisation. Regulation of the subcellular localisation of Tat-interactive protein 60 kDa via phosphorylation provides a novel means of controlling Tat-interactive protein 60 kDa function.

Pubmed ID: 17851107

Authors

  • Sapountzi V
  • Logan IR
  • Nelson G
  • Cook S
  • Robson CN

Journal

The international journal of biochemistry & cell biology

Publication Data

November 26, 2008

Associated Grants

  • Agency: Medical Research Council, Id: G0500966

Mesh Terms

  • Catalytic Domain
  • Cells, Cultured
  • Histone Acetyltransferases
  • Humans
  • Isoenzymes
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Protein Binding
  • Protein Kinase C-epsilon
  • Protein Transport
  • Tissue Distribution