RdgC/PP5-related phosphatases: novel components in signal transduction

Cell Signal. 1999 Aug;11(8):555-62. doi: 10.1016/s0898-6568(99)00032-7.


A great variety of cellular functions are regulated by protein serine/threonine phosphatases (PP). This review summarises the current knowledge of the structural features, patterns of expression and involvement in signal transduction pathways of protein serine/threonine phosphatases related to PP5 and RdgC. Designated now as PP5/RdgC subfamily by P. T. W. Cohen in her 1997 study published in Trends in Biochemical Sciences, (Vol. 22, pp. 245-251), this heterogeneous group comprises phosphatases PP5/PPT, containing regulatory domains with tetratricopeptide repeats, RdgC/PPEF, which possess Ca2+-binding EF hand-type sites, and, recently discovered in plants, PP7. PP5 is ubiquitously expressed and appears to be a multifunctional phosphatase involved in a number of different signalling pathways. In contrast, expression of RdgC/PPEF phosphatases and PP7 is confined primarily to specialised sensory cells in animals and plants, respectively, which may be indicative of their more specialised roles in sensory signal transduction.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins*
  • Drosophila Proteins*
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • Phosphoprotein Phosphatases / metabolism*
  • Signal Transduction*


  • Calcium-Binding Proteins
  • Drosophila Proteins
  • Nuclear Proteins
  • Phosphoprotein Phosphatases
  • protein phosphatase 5
  • rdgC protein, Drosophila