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- W1504605100 abstract "The major family of protein phosphatases that dephosphorylate serine and threonine residues includes PP1, PP2A, and the calciudcalmodulin-regulated protein phosphatase (PP2B, calcineurin-CNA, CMP), which were identified as enzyme activities in the cell cytosol. On further analysis, these novel phosphatases have been shown to carry out distinct cellular functions. A phylogenetic tree of the fully sequenced phosphatase catalytic subunits belonging to this family that is present in the human species and in the yeast Succbaromyces cereuisiue. Three novel protein phosphatases, termed human PP4 (originally designated PPX), S. cerevzszae SIT4, and PPG, show about 60% identity to PP2A and perform different cellular roles to PP2A. Human PP5 and yeast PPT comprise a catalytic domain preceded by a long N-terminal domain that contains four 34-amino-acid or tetratricopeptide repeat (TPR) motifs. Protein Phosphatase Y (PPY) was identified in Drosophila melanogaster and because no homologs in mammals or yeast have as yet been identified, it is necessary to study Drosophila to investigate the function of this protein phosphatase. The functions of several novel protein phosphatases in the major family of protein serinelthreonine phosphatases are beginning to be delineated. Only a few of the novel protein phosphatases have been tested for inhibition by okadaic acid and microcystin—the tumor promoters. Although a number of novel protein phosphatases, such as PP4 and PPS, are found in all tissues, some are tissue specific." @default.
- W1504605100 created "2016-06-24" @default.
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- W1504605100 date "1996-01-01" @default.
- W1504605100 modified "2023-09-26" @default.
- W1504605100 title "Novel Protein Phosphatases That May Participate in Cell Signaling" @default.
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- W1504605100 doi "https://doi.org/10.1016/s1054-3589(08)60577-3" @default.
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