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

Lookup NU author(s): Dr Vasileia Sapountzi, Dr Ian Logan, Dr Glyn NelsonORCiD, Susan Cook, Professor Craig Robson

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Abstract

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 Cε. In vitro, protein kinase Cε 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 Cε. 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 Cε phosphorylation sites on Tat-interactive protein 60 kDa are important for its subcelullar 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. © 2007 Elsevier Ltd. All rights reserved.

Publication metadata

Author(s): Sapountzi V, Logan IR, Nelson G, Cook S, Robson CN

Publication type: Article

Publication status: Published

Journal: International Journal of Biochemistry & Cell Biology

Year: 2008

Volume: 40

Issue: 2

Pages: 236-244

ISSN (print): 1357-2725

ISSN (electronic): 1878-5875

Publisher: Pergamon

URL: http://dx.doi.org/10.1016/j.biocel.2007.07.017

DOI: 10.1016/j.biocel.2007.07.017

PubMed id: 17851107

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