J. Vidal et al., LIGHT-DEPENDENT PHOSPHORYLATION OF PHOSPHOENOLPYRUVATE CARBOXYLASE AND ITS ROLE IN THE REGULATION OF C-4 PHOTOSYNTHESIS, Comptes rendus de l'Academie des sciences. Serie 3, Sciences de la vie, 319(11), 1996, pp. 1049-1053
This paper deals with the regulatory phosphorylation for the C-4 cycle
enzyme, cytosolic phosphoenolpyruvate carboxylase (PEPC) in mesophyll
cells from C-4 plants. Emphasis is put on the organization of the lig
ht signal-transduction chain which upregulates PEPC-kinase activity an
d the phosphorylation of PEPC. Initiation of the signalling pathway in
mesophyll cells involves 3-P-glycerate formed in the Calvin cycle of
the neighbouring bundle sheath cells. Downstream elements: cytosolic p
H, tonoplast InsP3-gated calcium channel, cytosolic calcium, a calcium
-dependent protein kinase and the calcium-independent PEPC-kinase have
been identified by a confocal microscopy/flux cytometry/protoplast ph
armacology approach. The post-translational modulation of PEPC strongl
y iinfluences its regulation by photosynthesis-related metabolites (L-
malate, feedback inhibitor and glucose-6P, allosteric activator). The
physiological significance of this process is discussed in the context
of C-4 photosynthesis.