Toggle Main Menu Toggle Search

Open Access padlockePrints

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


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


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


DOI: 10.1016/j.biocel.2007.07.017

PubMed id: 17851107


Altmetrics provided by Altmetric