Abstract
Protein phosphatase 5 (PP5) is a serine/threonine protein phosphatase that regulates many cellular functions including steroid hormone signaling, stress response, proliferation, apoptosis, and DNA repair. PP5 is also a co-chaperone of the heat shock protein 90 molecular chaperone machinery that assists in regulation of cellular signaling pathways essential for cell survival and growth. PP5 plays a significant role in survival and propagation of multiple cancers, which makes it a promising target for cancer therapy. Though there are several naturally occurring PP5 inhibitors, none is specific for PP5. Here, we review the roles of PP5 in cancer progression and survival and discuss the unique features of the PP5 structure that differentiate it from other phosphoprotein phosphatase (PPP) family members and make it an attractive therapeutic target.
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Acknowledgments
The authors are grateful to their colleagues Dimitra Bourboulia, John D. Chisholm, Timothy A. Haystead, and Gennady Bratslavsky for their scientific contributions.
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This work was partly supported by the National Institute of General Medical Sciences of the NIH grant R01GM124256 (M.M.). This work was also supported by funds from the SUNY Upstate Medical University, the Upstate Foundation, and the Carol M. Baldwin Breast Cancer Fund (M.M.) and in part by the Urology Care Foundation Research Scholar Award Program and American Urological Association (M.M.).
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Sager, R.A., Dushukyan, N., Woodford, M. et al. Structure and function of the co-chaperone protein phosphatase 5 in cancer. Cell Stress and Chaperones 25, 383–394 (2020). https://doi.org/10.1007/s12192-020-01091-3
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DOI: https://doi.org/10.1007/s12192-020-01091-3