Multisite phosphorylation of 14-3-3 proteins by calcium-dependent protein kinases

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Multisite phosphorylation of 14-3-3 proteins by calcium-dependent protein kinases.

Plant 14-3-3 proteins are phosphorylated at multiple sites in vivo; however, the protein kinase(s) responsible are unknown. Of the 34 CPK (calcium-dependent protein kinase) paralogues in Arabidopsis thaliana, three (CPK1, CPK24 and CPK28) contain a canonical 14-3-3-binding motif. These three, in addition to CPK3, CPK6 and CPK8, were tested for activity against recombinant 14-3-3 proteins χ and ...

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BACKGROUND The 14-3-3 proteins are structurally conserved throughout eukaryotes and participate in protein kinase signaling. All 14-3-3 proteins are known to bind to evolutionally conserved phosphoserine-containing motifs (modes 1 and/or 2) with high affinity. In Trypanosoma brucei, 14-3-3I and II play pivotal roles in motility, cytokinesis and the cell cycle. However, none of the T. brucei 14-...

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Inhibition of calcium/calmodulin-dependent protein kinase kinase by protein 14-3-3.

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Modelling cellular signal communication mediated by phosphorylation dependent interaction with 14-3-3 proteins.

The 14-3-3 proteins are important effectors of Ser/Thr phosphorylation in eukaryotic cells. Using mathematical modelling we investigated the roles of these proteins as effectors in signalling pathways that involve multi-phosphorylation events. We defined optimal conditions for positive and negative cross-talk. Particularly, synergistic signal interaction was evident at very different sets of bi...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2014

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj20130035