Tyrosine phosphorylation of WW proteins

Exp Biol Med (Maywood). 2015 Mar;240(3):375-82. doi: 10.1177/1535370214565991. Epub 2015 Jan 26.

Abstract

A number of key regulatory proteins contain one or two copies of the WW domain known to mediate protein-protein interaction via proline-rich motifs, such as PPxY. The Hippo pathway components take advantage of this module to transduce tumor suppressor signaling. It is becoming evident that tyrosine phosphorylation is a critical regulator of the WW proteins. Here, we review the current knowledge on the involved tyrosine kinases and their roles in regulating the WW proteins.

Keywords: Hippo pathway; cell fate decision-making; non-receptor tyrosine kinases; protein tyrosine phosphorylation; protein–protein interaction.

Publication types

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

MeSH terms

  • Humans
  • Oxidoreductases / metabolism*
  • Phosphorylation
  • Protein Binding / physiology
  • Protein Interaction Domains and Motifs / physiology
  • Protein-Tyrosine Kinases / physiology
  • Signal Transduction / physiology*
  • Tumor Suppressor Proteins / metabolism*
  • Tyrosine / metabolism*
  • WW Domain-Containing Oxidoreductase

Substances

  • Tumor Suppressor Proteins
  • Tyrosine
  • Oxidoreductases
  • WW Domain-Containing Oxidoreductase
  • WWOX protein, human
  • Protein-Tyrosine Kinases