1992
DOI: 10.1016/s0015-3796(11)80013-2
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The Regulation of the Activity of Soluble Starch Synthase in Spinach Leaves by a Calcium-Calmodulin Dependent Protein Kinase

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Cited by 7 publications
(3 citation statements)
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“…In the case of PHO1, six phosphorylation sites were identified, five of which are closely clustered together in a highly acidic region of the protein. Dreier et al (1992) showed that SS activity could be stimulated by ATP and that this might involve a calcium-calmodulindependent protein kinase, though there was no indication of which isoforms of SS were involved. The L78 region of PHO1 represents a large insertion that is typical for PHO1 in plastids of higher plants, but is not observed in the cytosolic isozyme nor in the well-studied glycogen phosphorylase.…”
Section: Regulation Of Protein Complex Formation By Protein Phosphorymentioning
confidence: 99%
“…In the case of PHO1, six phosphorylation sites were identified, five of which are closely clustered together in a highly acidic region of the protein. Dreier et al (1992) showed that SS activity could be stimulated by ATP and that this might involve a calcium-calmodulindependent protein kinase, though there was no indication of which isoforms of SS were involved. The L78 region of PHO1 represents a large insertion that is typical for PHO1 in plastids of higher plants, but is not observed in the cytosolic isozyme nor in the well-studied glycogen phosphorylase.…”
Section: Regulation Of Protein Complex Formation By Protein Phosphorymentioning
confidence: 99%
“…The presence of calmodulin in plastids implies a role for calmodulin in starch biosynthesis and degradation during plant growth and differentiation (Mitsui et al 1984;Preusser et al 1988;Dreier et al 1992), possibly by reversible, Ca 2 + -dependent, phosphorylation of proteins as was described for amyloplasts of sycamore cells (Ranjeva & Boudet 1987). In Nicotiana tabacum and Datura innoxia cell cultures, a protein kinase was isolated from plastids and the activity of this enzyme correlates with rapid cell proliferation and starch accumulation (Bacher et al 1985).…”
Section: Discussionmentioning
confidence: 99%
“…Importantly, Makhmoudova et al (2014) for these residues and their regulation. Dreier et al (1992) showed that SS activity could be stimulated by ATP and that this might involve a calcium-calmodulindependent protein kinase, though there was no indication of which isoforms of SS were involved. Whether the same CDPKs are involved in regulating glucan chain elongation and branching remains speculative at this stage.…”
Section: Regulation Of Protein Complex Formation By Protein Phosphorymentioning
confidence: 99%