ArticlePloS one2012
Phospholipid mediated activation of calcium dependent protein kinase 1 (CaCDPK1) from chickpea: a new paradigm of regulation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Arabidopsis PLANT U-BOX44 down-regulates osmotic stress signaling by mediating Ca2+-DEPENDENT PROTEIN KINASE4 degradation.The Plant cell · 2023Article
- A nanoelectronics-blood-based diagnostic biomarker for myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS).Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Improving Salt Tolerance of Chickpea Using Modern Genomics Tools and Molecular Breeding.Current genomics · 2017Review
- Transmembrane START domain proteins: in silico identification, characterization and expression analysis under stress conditions in chickpea (Cicer arietinum L.).Plant signaling & behavior · 2016Article
- Genome-Wide Identification and Expression Analysis of Calcium-dependent Protein Kinase in Tomato.Frontiers in plant science · 2016Article
- Calcium-dependent protein kinases: hubs in plant stress signaling and development.Plant physiology · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Phospholipids, the major structural components of membranes, can also have functions in regulating signaling pathways in plants under biotic and abiotic stress. The effects of adding phospholipids on the activity of stress-induced calcium dependent protein kinase (CaCDPK1) from chickpea are reported here. Both autophosphorylation as well as phosphorylation of the added substrate were enhanced specifically by phosphatidylcholine and to a lesser extent by phosphatidic acid, but not by phosphatidylethanolamine. Diacylgylerol, the neutral lipid known to activate mammalian PKC, stimulated CaCDPK1 but at higher concentrations. Increase in V(max) of the enzyme activity by these phospholipids significantly decreased the K(m) indicating that phospholipids enhance the affinity towards its substrate. In the absence of calcium, addition of phospholipids had no effect on the negligible activity of the enzyme. Intrinsic fluorescence intensity of the CaCDPK1 protein was quenched on adding PA and PC. Higher binding affinity was found with PC (K(½) = 114 nM) compared to PA (K(½) = 335 nM). We also found that the concentration of PA increased in chickpea plants under salt stress. The stimulation by PA and PC suggests regulation of CaCDPK1 by these phospholipids during stress response.
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