Evolution of protein phosphatases in plants and animals

Abstract

Protein phosphorylation appears to be a universal mechanism of protein regulation. Genomics has provided the means to compile inventories of protein phosphatases across a wide selection of organisms and this has supplied insights into the evolution of this group of enzymes. Protein phosphatases evolved independently several times yielding the groups we observe today. Starting from a core catalytic domain, phosphatases evolved by a series of gene duplication events and by adopting the use of regulatory subunits and/or fusion with novel functional modules or domains. Recent analyses also suggest that the serine/threonine specific enzymes are more ancient than the PTPs (protein tyrosine phosphatases). It is likely that the latter played a key role at the onset of metazoan evolution in conjunction with the tremendous expansion of tyrosine kinases and PTPs at this point. In the present review, we discuss the evolution of the PTPs, the serine/threonine specific PPP (phosphoprotein phosphatase) and PPM (metallo-dependent protein phosphatase) families and the more recently discovered phosphatases that utilize an aspartate-based catalytic mechanism. We will also highlight examples of convergent evolution and several phosphatases which are unique to plants.

Convergent evolution of two mammalian neuronal enhancers by sequential exaptation of unrelated retroposons

“…There are several morphological and functional examples of convergent evolution, such as the development of wings in birds and bats, eyes in cephalopods and mammals, and immune systems in jawed and jawless fishes (23). Some examples of convergent molecular evolution at the protein coding level have also been reported, including the origin of visual pigment genes in fishes and humans (24) and protein phosphatases in animals and plants (25). In the case reported here, a MaLR and a CORE-SINE retroposon independently evolved into functional arcuate-specific enhancers of POMC in mammals.…”

Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates

“…All three glucan phosphatases are members of the protein tyrosine phosphatase (PTP) superfamily and are classified in the heterogeneous subgroup called dual-specificity phosphatases (DSPs) that share a conserved CX 5 R catalytic motif (11,(52)(53)(54)(55)(56). Most DSPs dephosphorylate pTyr and pSer/Thr residues of proteins, while others dephosphorylate non-proteinaceous substrates such as lipids, nucleic acids, or glucans (53,54,56).…”

Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation

“…During the 'genomic era,' an enormous number of different protein kinases and phospho-protein (P-protein) phosphatases were identified, and reversible protein phosphorylation has been shown to be involved in regulating many fundamental cellular processes. It has been reported that the combination of genes encoding protein kinases and P-protein phosphatases constitute between 2 and 4% of the total number of genes in a typical eukaryotic genome [18]. Saccharomyces cerevisiae has genes for 113 protein kinases while the Homo sapiens has 518 such genes [19].…”