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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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Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
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Mid-range Ca2+ signalling mediated by functional coupling between store-operated Ca2+ entry and IP3-dependent Ca2+

Raphaël Courjaret1, Khaled Machaca1

  • 1Department of Physiology and Biophysics, Weill Cornell Medical College in Qatar, Education City, Qatar Foundation, PO Box 24144, Doha, Qatar.

Nature Communications
|May 29, 2014
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Summary

This study reveals how calcium (Ca2+) signals travel mid-range without global rise. It shows intricate coupling of inositol 1,4,5 trisphosphate receptors, SERCA pumps, and store-operated calcium entry regulates spatially distant cellular effectors.

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Area of Science:

  • Cellular Biology
  • Physiology
  • Biochemistry

Background:

  • Calcium (Ca2+) signals exhibit diverse spatial and temporal dynamics, crucial for cellular functions.
  • While microdomain and whole-cell Ca2+ signaling are understood, mid-range Ca2+ signal regulation remains unclear.
  • Activating spatially distant effectors without a global Ca2+ rise presents a significant regulatory challenge.

Purpose of the Study:

  • To investigate the mechanism of mid-range Ca2+ signaling.
  • To elucidate the role of inositol 1,4,5 trisphosphate receptors, SERCA pumps, and store-operated Ca2+ entry (SOCE) in this process.
  • To understand how local Ca2+ signals are regulated to activate distant effectors.

Main Methods:

  • Investigated the interplay between IP3 receptors, SERCA pumps, and SOCE.
  • Utilized techniques to track Ca2+ dynamics within cellular compartments.
  • Examined the functional consequences of this coupling on Ca2+-activated Cl- channels (CaCCs).

Main Results:

  • Demonstrated an intricate coupling between SOCE, SERCA, and IP3 receptors for mid-range Ca2+ signaling.
  • Showed that Ca2+ entering via SOCE is taken up by SERCA into the ER lumen and re-released by IP3Rs.
  • Identified that this mechanism activates spatially distant CaCCs, influencing cell membrane potential.

Conclusions:

  • Functional coupling between SOCE, SERCA, and IP3R enables efficient mid-range Ca2+ signaling.
  • This pathway limits local Ca2+ diffusion and channels Ca2+ through the ER lumen.
  • The regulated activation of distal CaCCs by this mechanism plays a role in cellular electrophysiology.