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- W87486054 abstract "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." @default.
- W87486054 created "2016-06-24" @default.
- W87486054 creator A5032352102 @default.
- W87486054 creator A5062944007 @default.
- W87486054 date "1999-08-01" @default.
- W87486054 modified "2023-09-27" @default.
- W87486054 title "RdgC/PP5-Related Phosphatases" @default.
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- W87486054 doi "https://doi.org/10.1016/s0898-6568(99)00032-7" @default.
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