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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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CBL-CIPK module-mediated phosphoregulation: facts and hypothesis.

Sibaji K Sanyal1, Swati Mahiwal1, Deepti M Nambiar1

  • 1Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi 110021, India.

The Biochemical Journal
|March 5, 2020
PubMed
Summary

Calcium (Ca2+) signaling in plants involves the CBL-CIPK module, a sensor-relay system. This study overviews how phosphorylation regulates this module and its targets, including the role of phosphatases.

Keywords:
CBL–CIPKLC–MS/MSphosphatasesphosphoproteomicsphosphosites

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Area of Science:

  • Plant molecular biology
  • Cell signaling
  • Biochemistry

Background:

  • Calcium (Ca2+) signaling is crucial in plants, utilizing efficient signal decoders.
  • The CBL-CIPK module, comprising CBL proteins and CIPK kinases, acts as a sensor-relay system in plant signal transduction.
  • CBL proteins feature unique Ca2+ sensing EF-hands, while CIPKs are Ser/Thr kinases.

Purpose of the Study:

  • To analyze substrate regulation by the CBL-CIPK module from a phosphorylation perspective.
  • To identify potential CIPK phosphorylation sites on substrates.
  • To elucidate the role of phosphatases in modulating the CBL-CIPK module and its targets.

Main Methods:

  • Analysis of existing data on substrate regulation by the CBL-CIPK module.
  • Prediction of CIPK-mediated phosphorylation sites on identified substrates.
  • Review of literature on the role of phosphatases in the CBL-CIPK signaling pathway.

Main Results:

  • Phosphorylation is a key mechanism for regulating the CBL-CIPK module's function and interactions.
  • Specific phosphorylation sites on substrates targeted by CIPKs were predicted.
  • Phosphatases play a significant role in reversing CIPK-mediated phosphorylation, thus modulating signaling.

Conclusions:

  • The CBL-CIPK module's phosphoregulation mechanism is central to plant signaling.
  • Understanding these phosphorylation events is vital for comprehending plant responses to stimuli.
  • The interplay between CIPKs and phosphatases fine-tunes calcium signal transduction pathways.