Nuclear localization of protein phosphatase 5 is dependent on the carboxy-terminal region

Emma B. Borthwick, Tamás Zeke, Alan R. Prescott, Patricia T. W. Cohen

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

Endogenous and overexpressed protein phosphatase 5 (PP5) localizes to the nucleus and cytoplasm of HeLa cells, while the overexpressed TPR domain of PP5 is restricted to the cytoplasm. Deletion and mutational analysis of human PP5 demonstrates that the C-terminal amino acids 420-499 are essential for nuclear localization and PP5 activity is not required. Since the phosphatase domain terminates at 473, these studies suggest that the highly conserved section (476-491) with the eukaryotic consensus FXAVPHPXΦXPMAYAN is required for nuclear localization of PP5. Bacterially expressed PP5 is inhibited by several tumor promoters but not by the anticancer drug fostriecin.

Original languageEnglish
Pages (from-to)279-284
Number of pages6
JournalFEBS Letters
Volume491
Issue number3
Early online date1 Mar 2001
DOIs
Publication statusPublished - 2 Mar 2001

Keywords

  • Cell signalling
  • Nuclear localization
  • Protein phosphatase
  • Tetratricopeptide repeat
  • Tumor promoter

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