Ppp5 (protein phosphatase 5) is a serine/threonine protein phosphatase that has been conserved throughout eukaryotic evolution. In mammalian cells, FLAG-tagged Ppp5 and endogenous Ppp5 are found to interact with endogenous Hsp (heat-shock protein) 70, as well as Hsp90. Incubation of cells with arachidonic acid or the microtubule-depolymerizing agent, nocodazole, causes loss of interaction of Hsp70 and Hsp90 with FLAG-tagged Ppp5 and increase of Ppp5 activity. In response to the same treatments, endogenous Ppp5 undergoes proteolytic cleavage of the N- and C-termini, with the subsequent appearance of high-molecular-mass species. The results indicate that Ppp5 is activated by proteolysis on dissociation from Hsps, and is destroyed via the proteasome after ubiquitination. Cleavage at the C-terminus removes a nuclear localization sequence, allowing these active cleaved forms of Ppp5 to translocate to the cytoplasm. The response of Ppp5 to arachidonic acid and nocodazole suggests that Ppp5 may be required for stress-related processes that can sometimes cause cell-cycle arrest, and leads to the first description for in vivo regulation of Ppp5 activity.
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Research Article|
December 14 2004
Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole Available to Purchase
Tamás ZEKE;
Tamás ZEKE
1Medical Research Council Protein Phosphorylation Unit, Division of Cell Signalling, School of Life Sciences, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
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Nick MORRICE;
Nick MORRICE
1Medical Research Council Protein Phosphorylation Unit, Division of Cell Signalling, School of Life Sciences, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
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Cristina VÁZQUEZ-MARTIN;
Cristina VÁZQUEZ-MARTIN
1Medical Research Council Protein Phosphorylation Unit, Division of Cell Signalling, School of Life Sciences, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
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Patricia T. W. COHEN
Patricia T. W. COHEN
1
1Medical Research Council Protein Phosphorylation Unit, Division of Cell Signalling, School of Life Sciences, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
April 27 2004
Revision Received:
August 26 2004
Accepted:
September 21 2004
Accepted Manuscript online:
September 21 2004
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 385 (1): 45–56.
Article history
Received:
April 27 2004
Revision Received:
August 26 2004
Accepted:
September 21 2004
Accepted Manuscript online:
September 21 2004
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Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole
Citation
Tamás ZEKE, Nick MORRICE, Cristina VÁZQUEZ-MARTIN, Patricia T. W. COHEN; Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole. Biochem J 1 January 2005; 385 (1): 45–56. doi: https://doi.org/10.1042/BJ20040690
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