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- W433790587 abstract "Reversible phosphorylation is a key mechanism for the control of intercellular events in eukaryotic cells. In animal cells, Ca2+/CaM-dependent protein phosphorylation and dephosphorylation are implicated in the regulation of a number of cellular processes. However, little is known on the functions of Ca2+/CaM-dependent protein kinases and phosphatases in Ca2+ signaling in plants. From an Arabidopsis expression library, we isolated cDNA encoding a dual-specificity protein phosphatase 1 (DsPTP1), which is capable of hydrolyzing both phosphoserine/threonine and phosphotyrosine residues of the substrates. Using a gel overlay assay, we identified two Ca2+-dependent CaM binding domains. Specific binding of CaM to two CaMBD was confirmed by site-directed mutagenesis, a gel mobility shift assay, and a competition assay using a Ca2+/CaM-dependent enzyme. At increasing concentrations of CaM, the biochemical activity of DsPTP1 on the pNPP substrate was increased, whereas activity on the phosphotyrosine of MBP was inhibited. Based on these findings, we propose that the Ca2+ signaling pathway mediated by CaM cross-talks with a protein phosphorylation signal pathway in plants via protein dephosphorylation [This work is supported by a grant from Plant Diversity Research Center (PF0330402-00) funded by MOST of Korean government]." @default.
- W433790587 created "2016-06-24" @default.
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- W433790587 date "2006-03-01" @default.
- W433790587 modified "2023-09-24" @default.
- W433790587 title "Interaction of a Dual‐Specificity Protein Phosphatase with Calmodulin in Regulating its Activity" @default.
- W433790587 doi "https://doi.org/10.1096/fasebj.20.5.a923" @default.
- W433790587 hasPublicationYear "2006" @default.
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