The pseudophosphatase STYX (serine/threonine/tyrosine interacting protein) is a catalytically inactive member of the protein tyrosine phosphatase family. We perform a phylogenetic analysis of STYX and ask how far does the pseudoenzyme status of STYX reaches in evolution. Based on our previous work, we use STYX as a showcase to discuss four basic modes of action that any given pseudoenzyme may exert. Our previous work on the effect of STYX on mitogen-activated protein kinase (MAPK) signaling led us to identify two complementary modes of action. On the one hand, STYX competes with active phosphatases for binding to MAPKs. On the other hand, STYX acts as a nuclear anchor for MAPKs, affecting their nucleo-cytoplasmic shuttling. Finally, we discuss our recent work on the regulation of FBXW7 by this pseudophosphatase and how it affects the ubiquitylation and degradation of its substrates. We discuss the biological significance of this regulatory mechanism and use it as an example for the versatility of pseudoenzymes that may divert away from merely regulating their active homologs.
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April 2017
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This artistic rendition shows an Atomic Force Microscopy tip probing the mechanics of an individual virus particle. The colour scale of the particle indicates the deformation and stress of the viral shell obtained with Finite Element Analysis. The applied force is monitored by focusing a laser beam at the end of the microcantilever. For more information please see study by Moreno-Madrid et al. in this issue, pages 499–511. Image provided by Pedro De Pablo.
Review Article|
April 13 2017
STYX: a versatile pseudophosphatase
Veronika Reiterer;
1Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Oslo, Norway
Correspondence: Veronika Reiterer (veronika.reiterer-farhan@medisin.uio.no), Krzysztof Pawłowski (krzysztof_pawlowski@sggw.pl) or Hesso Farhan (hesso.farhan@medisin.uio.no)
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Krzysztof Pawłowski;
2Department of Experimental Design and Bioinformatics, Warsaw University of Life Sciences, Warsaw, Poland
Correspondence: Veronika Reiterer (veronika.reiterer-farhan@medisin.uio.no), Krzysztof Pawłowski (krzysztof_pawlowski@sggw.pl) or Hesso Farhan (hesso.farhan@medisin.uio.no)
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Hesso Farhan
1Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Oslo, Norway
Correspondence: Veronika Reiterer (veronika.reiterer-farhan@medisin.uio.no), Krzysztof Pawłowski (krzysztof_pawlowski@sggw.pl) or Hesso Farhan (hesso.farhan@medisin.uio.no)
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Publisher: Portland Press Ltd
Received:
January 02 2017
Revision Received:
February 16 2017
Accepted:
February 20 2017
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem Soc Trans (2017) 45 (2): 449–456.
Article history
Received:
January 02 2017
Revision Received:
February 16 2017
Accepted:
February 20 2017
Citation
Veronika Reiterer, Krzysztof Pawłowski, Hesso Farhan; STYX: a versatile pseudophosphatase. Biochem Soc Trans 15 April 2017; 45 (2): 449–456. doi: https://doi.org/10.1042/BST20160279
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