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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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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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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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Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
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The calcium-signaling toolkit: Updates needed.

Charlotte Dubois1, Natalia Prevarskaya1, Fabien Vanden Abeele1

  • 1Inserm U1003, Equipe labellisée par la Ligue Nationale Contre le Cancer, SIRIC ONCOLille, Université des Sciences et Technologies de Lille (USTL), Villeneuve d'Ascq, 59650 France, Laboratory of Excellence, Ion Channels Science and Therapeutics, France.

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Summary

Calcium dysregulation, including ER calcium depletion or elevated cytosolic/mitochondrial calcium, triggers apoptosis. New research reveals ER calcium modulators impact other cell fate pathways, complicating apoptosis regulation.

Keywords:
ApoptosisAutophagyCalciumInhibitorSERCAUnfold Protein Response

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Physiology

Background:

  • Calcium ions (Ca2+) play a critical role in cellular processes.
  • Dysregulation of intracellular Ca2+ homeostasis is linked to cell death pathways.
  • The endoplasmic reticulum (ER) is a key organelle for Ca2+ storage and signaling.

Purpose of the Study:

  • To review the multifaceted role of Ca2+ in apoptosis.
  • To explore the complex interplay between Ca2+ signaling, ER stress, and autophagy in determining cell fate.
  • To identify limitations of current pharmacological tools and highlight the need for novel therapeutic agents.

Main Methods:

  • Literature review of studies investigating Ca2+ homeostasis and apoptosis.
  • Analysis of molecular compounds affecting Ca2+ signaling and cell fate pathways.
  • Examination of the interplay between Ca2+-mediated apoptosis, Unfolded Protein Response, and autophagy.

Main Results:

  • ER Ca2+ depletion or sustained cytosolic/mitochondrial Ca2+ elevation can initiate apoptosis.
  • ER Ca2+ modulators influence Ca2+-mediated and Ca2+-independent cell fate pathways.
  • Existing ER Ca2+ modulators often interfere with autophagy and Ca2+ signaling simultaneously.

Conclusions:

  • Intracellular Ca2+ regulation of apoptosis is more complex than previously understood.
  • A deeper understanding of the interplay between Ca2+, ER stress, and autophagy is crucial for cell fate determination.
  • Development of novel inhibitors that selectively target Ca2+ signaling without affecting autophagy is warranted.