Rethinking pseudokinases

Cell. 2008 Apr 18;133(2):204-5. doi: 10.1016/j.cell.2008.04.005.


Pseudokinases lack conservation of one or more of the catalytic residues in the kinase core and as a consequence are typically thought to be catalytically inactive. New work by Mukherjee et al. (2008) challenges this assumption. They show that the pseudokinase domain of CASK (Ca2+/calmodulin activated serine-threonine kinase) adopts an active conformation and displays catalytic activity in vivo.

Publication types

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

MeSH terms

  • Guanylate Kinases / chemistry
  • Guanylate Kinases / genetics
  • Guanylate Kinases / metabolism*
  • Humans
  • Phosphorylation
  • Protein Conformation
  • Protein Structure, Tertiary


  • CASK kinases
  • Guanylate Kinases