RdgC/PP5-related phosphatases: novel components in signal transduction.
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.
Andreeva
A V
AV
Research School of Biological and Molecular Sciences, Oxford Brookes University, Headington, UK. p0071233@brookes.ac.uk
Kutuzov
M A
MA
D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins; D029721:Drosophila Proteins; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D015398:Signal Transduction
D002135:Calcium-Binding Proteins; D029721:Drosophila Proteins; D009687:Nuclear Proteins; D010749:Phosphoprotein Phosphatases; C089641:protein phosphatase 5; C074643:rdgC protein, Drosophila