Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1984984 | The International Journal of Biochemistry & Cell Biology | 2008 | 9 Pages |
Abstract
Tat-interactive protein 60Â 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 60Â kDa is phosphorylated by protein kinase CÉ. In vitro, protein kinase CÉ phosphorylates Tat-interactive protein 60Â 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 60Â kDa and the interaction of Tat-interactive protein 60Â kDa with protein kinase CÉ. A phosphomimetic mutant Tat-interactive protein 60Â kDa has distinct subcellular localisation compared to the wild-type protein in whole cells. Taken together, these findings suggest that the protein kinase CÉ phosphorylation sites on Tat-interactive protein 60Â kDa are important for its subcelullar localisation. Regulation of the subcellular localisation of Tat-interactive protein 60Â kDa via phosphorylation provides a novel means of controlling Tat-interactive protein 60Â kDa function.
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Authors
Vasileia Sapountzi, Ian R. Logan, Glyn Nelson, Susan Cook, Craig N. Robson,