Sucrose‐phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves

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Abstract
Sucrose‐phosphate synthase (SPS) purified from spinach leaves harvested in the dark, was activated by mammalian protein phosphatase 2A (PP2A). Activation of SPS in a fraction from darkened spinach leaves was largely prevented by either okadaic acid or microcystin‐LR (specific inhibitors of PP1 and PP2A), while inhibitor‐2 (a PP1 inhibitor) or Mg2+ (essential for PP2C) were ineffective. In vivo, okadaic add and microcystin‐LR prevented the light‐induced activation of SPS and decreased sucrose biosynthesis and CO2 fixation. It is concluded that PP2A is the major SPS phosphatase in spinach. This study is the first to employ microcystin‐LR for modulating protein phosphorylation in vivo.