@article{528771857b6242cdbd9a8935b8880465,
title = "The dead phosphatases society: a review of the emerging roles of pseudophosphatases",
abstract = "Phosphatases are a diverse family of enzymes, comprising at least 10 distinct protein folds. Like most other enzyme families, many have sequence variations that predict an impairment or loss of catalytic activity classifying them as pseudophosphatases. Research on pseudoenzymes is an emerging area of interest, with new biological functions repurposed from catalytically active relatives. Here, we provide an overview of the pseudophosphatases identified to date in all major phosphatase families. We will highlight the degeneration of the various catalytic sequence motifs and discuss the challenges associated with the experimental determination of catalytic inactivity. We will also summarize the role of pseudophosphatases in various diseases and discuss the major challenges and future directions in this field.",
keywords = "dephosphorylation, phosphatase, pseudoenzymes, pseudophosphatase",
author = "Veronika Reiterer and Krzysztof Paw{\l}owski and Guillaume Desrochers and Arnim Pause and Sharpe, {Hayley J.} and Hesso Farhan",
note = "Funding Information: HJS is supported by a Sir Henry Dale Fellowship jointly funded by the Wellcome Trust and the Royal Society (109407). AP was financed by grants from the Canadian Institutes of Health Research (CIHR) [PJT-152966] and the Canadian Cancer Society Research Institute (CCSRI) [705376]. G.D. was supported by a postdoctoral training award from the Fonds de recherche du Qu?bec?Sant? (FRQS). KP was supported by the Polish National Agency for Scientific Exchange scholarship PPN/BEK/2018/1/00431. HF is supported by grants from the Norwegian Cancer Society (182815), and the Norwegian Research Council (262717) and from the Rakel og Otto-Kristian Bruun legat. Funding Information: HJS is supported by a Sir Henry Dale Fellowship jointly funded by the Wellcome Trust and the Royal Society (109407). AP was financed by grants from the Canadian Institutes of Health Research (CIHR) [PJT‐152966] and the Canadian Cancer Society Research Institute (CCSRI) [705376]. G.D. was supported by a postdoctoral training award from the Fonds de recherche du Qu{\'e}bec—Sant{\'e} (FRQS). KP was supported by the Polish National Agency for Scientific Exchange scholarship PPN/BEK/2018/1/00431. HF is supported by grants from the Norwegian Cancer Society (182815), and the Norwegian Research Council (262717) and from the Rakel og Otto‐Kristian Bruun legat. Publisher Copyright: {\textcopyright} 2020 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies",
year = "2020",
month = oct,
day = "1",
doi = "10.1111/febs.15431",
language = "English (US)",
volume = "287",
pages = "4198--4220",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "19",
}