A Ca2+‐dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize
- 4 May 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 302 (1) , 86-88
- https://doi.org/10.1016/0014-5793(92)80291-n
Abstract
In C4 plants the activity of phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is regulated by phosphorylation/dephosphorylation which is mediated by light/dark signals. The study using protein kinase inhibitors showed that the inhibition pattern of maize PEPC-protein kinase (PEPC-PK) is similar to that of myosin light chain kinase, a Ca(2+)-calmodulin-dependent PK. The kinase activity was also inhibited by EGTA and the inhibition was relieved by Ca2+. These results suggest that PEPC-PK is Ca(2+)-dependent in contrast with previous observations by other research groups.Keywords
This publication has 11 references indexed in Scilit:
- Illumination increases the phosphorylation state of maize leaf phospho enolpyruvate car☐ylase by causing an increase in the activity of a protein kinaseBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1991
- Posttranslational Regulation of Phosphoenolpyruvate Carboxylase in C4 and Crassulacean Acid Metabolism PlantsPlant Physiology, 1991
- Reversible light activation of the phosphoenolpyruvate carboxylase protein‐serine kinase in maize leavesFEBS Letters, 1990
- Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser15 with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malateFEBS Letters, 1990
- Regulatory seryl-phosphorylation of C4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leavesArchives of Biochemistry and Biophysics, 1989
- The phosphorylation of Sorghum leaf phosphoenolpyruyate carboxylase is a Ca++-calmodulin dependent processBiochemical and Biophysical Research Communications, 1988
- Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-independent fragments.Journal of Biological Chemistry, 1987
- A Calcium-Dependent but Calmodulin-Independent Protein Kinase from SoybeanPlant Physiology, 1987
- K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinasesBiochemical and Biophysical Research Communications, 1986
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976