The role of pseudophosphatases as signaling regulators

Biochim Biophys Acta Mol Cell Res. 2019 Jan;1866(1):167-174. doi: 10.1016/j.bbamcr.2018.07.021. Epub 2018 Aug 2.

Abstract

Pseudophosphatases are atypical members of the protein tyrosine phosphatase superfamily. Mutations within their catalytic signature motif render them catalytically inactive. Despite this lack of catalytic function, pseudophosphatases have been implicated in various diseases such as Charcot Marie-Tooth disorder, cancer, metabolic disorder, and obesity. Moreover, they have roles in various signaling networks such as spermatogenesis, apoptosis, stress response, tumorigenesis, and neurite differentiation. This review highlights the roles of pseudophosphatases as essential regulators in signaling cascades, providing insight into the function of these catalytically inactive enzymes.

Keywords: Dead enzymes; MK-STYX [MAPK (mitogen-activated protein kinase) phosphoserine/threonine/tyrosine-binding protein]; Protein tyrosine phosphatases; Pseudoenzymes; Pseudophosphatases; STYX (phosphor/serine/threonine/tyrosine-binding protein).

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins / metabolism*
  • Apoptosis Regulatory Proteins / physiology
  • Caenorhabditis elegans Proteins
  • Charcot-Marie-Tooth Disease
  • Humans
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Intracellular Signaling Peptides and Proteins / physiology
  • Metabolic Diseases
  • Neoplasms
  • Nuclear Proteins / metabolism*
  • Nuclear Proteins / physiology
  • Obesity
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphotransferases / metabolism
  • Protein Tyrosine Phosphatases / metabolism*
  • Protein Tyrosine Phosphatases / physiology
  • Signal Transduction

Substances

  • Apoptosis Regulatory Proteins
  • Caenorhabditis elegans Proteins
  • Intracellular Signaling Peptides and Proteins
  • Nuclear Proteins
  • STYX protein, human
  • STYXL1 protein, human
  • Phosphotransferases
  • Phosphoric Monoester Hydrolases
  • Protein Tyrosine Phosphatases