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Biochemical and immunological data establish serine 170 as an additional site on sucrose synthase for in-vivo phosphorylation by CDPK. Moreover, phosphorylation at this site is implicated in the regulation of sucrose synthase stability during sink-to-source transitions by targeting the enzyme to the proteasome degradation pathway.
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Hardin S.C., Tang G.-Q., Scholz A., Holtgraewe D., Winter H., Huber S.C. Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis. Plant J. 35:2003;588-603 Biochemical and immunological data establish serine 170 as an additional site on sucrose synthase for in-vivo phosphorylation by CDPK. Moreover, phosphorylation at this site is implicated in the regulation of sucrose synthase stability during sink-to-source transitions by targeting the enzyme to the proteasome degradation pathway.
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Phosphorylation of the Arabidopsis dual-affinity nitrate transporter CHL1 at threonine residue 101 is shown to convert the action of the transporter from a low-affinity to a high-affinity mode. Thus, dephosphorylation may facilitate the rapid downregulation of uptake activity in response to the accumulation of reduced nitrogen metabolites or other environmental conditions.
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A comprehensive proteomic approach to the identification of phosphorylation sites yields a rich source of intriguing in-vivo protein kinase substrates that occur as integral plasma-membrane proteins in Arabidopsis. Among the more than 200 phosphopeptides identified are many membrane transporters, receptor-like kinases and enzymes, supporting the notion that phosphorylation is important in regulating events at the plasma membrane.
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Nühse T.S., Stensballe A., Jensen O.N., Peck S.C. Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2:2003;1234-1243 A comprehensive proteomic approach to the identification of phosphorylation sites yields a rich source of intriguing in-vivo protein kinase substrates that occur as integral plasma-membrane proteins in Arabidopsis. Among the more than 200 phosphopeptides identified are many membrane transporters, receptor-like kinases and enzymes, supporting the notion that phosphorylation is important in regulating events at the plasma membrane.
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An intermolecular disulfide bridge that is known to reduce enzymatic activity was shown to occur in vivo. When tuber sucrose content was increased by physiological and genetic manipulations, AGPase was activated by reduction of the disulfide bridge. This important study established that redox modulation, as opposed to allosteric control, is the mechanism that controls starch synthesis in response to changes in sugar supply.
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