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

doi:10.1016/S0014-5793(01)02177-9

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 journal › Article › peer-review

52 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 language	English
Pages (from-to)	279-284
Number of pages	6
Journal	FEBS Letters
Volume	491
Issue number	3
Early online date	1 Mar 2001
DOIs	https://doi.org/10.1016/S0014-5793(01)02177-9
Publication status	Published - 2 Mar 2001

Keywords

Cell signalling
Nuclear localization
Protein phosphatase
Tetratricopeptide repeat
Tumor promoter

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(01)02177-9

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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.",

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AU - Zeke, Tamás

AU - Prescott, Alan R.

AU - Cohen, Patricia T. W.

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AB - 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.

KW - Cell signalling

KW - Nuclear localization

KW - Protein phosphatase

KW - Tetratricopeptide repeat

KW - Tumor promoter

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

Abstract

Keywords

ASJC Scopus subject areas

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