Intracellular Ca2+ Sensing: Roles from Ca2+ Stores to Cytosolic Microdomains

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Signaling".

Deadline for manuscript submissions: closed (28 February 2023) | Viewed by 6913

Special Issue Editors


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Guest Editor
CarMeN Laboratory, IRIS Team, University Lyon 1, INSERM U1060, 69500 Bron, France
Interests: Ca2+ homeostasis; excitation–contraction coupling; cardiac muscle; skeletal muscle; B lymphocyte; ryanodine receptors; TRP channels; reticulum–mitochondria contact sites
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Guest Editor
CarMeN Laboratory, IRIS Team, University Lyon 1, INSERM U1060, 69500 Bron, France
Interests: cardiovascular diseases; cancer; Ca2+ homeostasis; TRP channels; reticulum-mitochondria contact sites; mitochondria; gene regulation; metabolism

Special Issue Information

Dear Colleagues,

Intracellular calcium fluxes are integrated by the molecular network as information, thus defined as calcium signals, and participate in the orchestration of multiple cellular processes. The biophysical properties of Ca2+ signals (localization, intensity, time modality) encode biological information. In the last several years, genetically modified biosensors and breakthroughs in the resolution of photon microscopes have improved our understanding of functional units within intracellular compartments, defined as micro- or nano-domains. Some of these domains are formed by contact sites between compartments (e.g., mitochondria-associated membranes, plasma-to-ER contract sites) and are especially subject to calcium fluxes, but other domains have also emerged and could promote calcium signals to control their activity.

While calcium signals carry information, the release of calcium content in calcium stores (cellular compartments with a rich Ca2+ content at steady state) also create a modification in the equilibrium that can also encode a signal which, in turn, will trigger hidden biological functions. As an example, calsequestrin, the main sarcoplasmic reticulum Ca2+ binding protein of striated muscle, has a dual function providing a large pool of fast-releasable Ca2+ during excitation–contraction coupling and modulating the activity of ryanodine receptors according to the current luminal Ca2+ concentration.

This Special Issue will examine the identification of new developments in calcium signaling in microdomains and calcium stores.

Dr. Sylvie Ducreux
Dr. Gabriel Bidaux
Guest Editors

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Keywords

  • calcium channel
  • mitochondria and calcium
  • sarcoplasmic reticulum and calcium
  • mitochondria-associated ER membrane
  • calcium signaling
  • calcium binding protein
  • calcium microdomains

Published Papers (2 papers)

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Research

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22 pages, 7521 KiB  
Article
TRPV1 Channels Are New Players in the Reticulum–Mitochondria Ca2+ Coupling in a Rat Cardiomyoblast Cell Line
by Nolwenn Tessier, Mallory Ducrozet, Maya Dia, Sally Badawi, Christophe Chouabe, Claire Crola Da Silva, Michel Ovize, Gabriel Bidaux, Fabien Van Coppenolle and Sylvie Ducreux
Cells 2023, 12(18), 2322; https://0-doi-org.brum.beds.ac.uk/10.3390/cells12182322 - 20 Sep 2023
Cited by 3 | Viewed by 1655
Abstract
The Ca2+ release in microdomains formed by intercompartmental contacts, such as mitochondria-associated endoplasmic reticulum membranes (MAMs), encodes a signal that contributes to Ca2+ homeostasis and cell fate control. However, the composition and function of MAMs remain to be fully defined. Here, [...] Read more.
The Ca2+ release in microdomains formed by intercompartmental contacts, such as mitochondria-associated endoplasmic reticulum membranes (MAMs), encodes a signal that contributes to Ca2+ homeostasis and cell fate control. However, the composition and function of MAMs remain to be fully defined. Here, we focused on the transient receptor potential vanilloid 1 (TRPV1), a Ca2+-permeable ion channel and a polymodal nociceptor. We found TRPV1 channels in the reticular membrane, including some at MAMs, in a rat cardiomyoblast cell line (SV40-transformed H9c2) by Western blotting, immunostaining, cell fractionation, and proximity ligation assay. We used chemical and genetic probes to perform Ca2+ imaging in four cellular compartments: the endoplasmic reticulum (ER), cytoplasm, mitochondrial matrix, and mitochondrial surface. Our results showed that the ER Ca2+ released through TRPV1 channels is detected at the mitochondrial outer membrane and transferred to the mitochondria. Finally, we observed that prolonged TRPV1 modulation for 30 min alters the intracellular Ca2+ equilibrium and influences the MAM structure or the hypoxia/reoxygenation-induced cell death. Thus, our study provides the first evidence that TRPV1 channels contribute to MAM Ca2+ exchanges. Full article
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14 pages, 881 KiB  
Review
Sarcoplasmic Reticulum Ca2+ Buffer Proteins: A Focus on the Yet-To-Be-Explored Role of Sarcalumenin in Skeletal Muscle Health and Disease
by Elena Conte, Giorgia Dinoi, Paola Imbrici, Annamaria De Luca and Antonella Liantonio
Cells 2023, 12(5), 715; https://0-doi-org.brum.beds.ac.uk/10.3390/cells12050715 - 24 Feb 2023
Cited by 2 | Viewed by 4719
Abstract
Sarcalumenin (SAR) is a luminal Ca2+ buffer protein with high capacity but low affinity for calcium binding found predominantly in the longitudinal sarcoplasmic reticulum (SR) of fast- and slow-twitch skeletal muscles and the heart. Together with other luminal Ca2+ buffer proteins, [...] Read more.
Sarcalumenin (SAR) is a luminal Ca2+ buffer protein with high capacity but low affinity for calcium binding found predominantly in the longitudinal sarcoplasmic reticulum (SR) of fast- and slow-twitch skeletal muscles and the heart. Together with other luminal Ca2+ buffer proteins, SAR plays a critical role in modulation of Ca2+ uptake and Ca2+ release during excitation–contraction coupling in muscle fibers. SAR appears to be important in a wide range of other physiological functions, such as Sarco-Endoplasmic Reticulum Calcium ATPase (SERCA) stabilization, Store-Operated-Calcium-Entry (SOCE) mechanisms, muscle fatigue resistance and muscle development. The function and structural features of SAR are very similar to those of calsequestrin (CSQ), the most abundant and well-characterized Ca2+ buffer protein of junctional SR. Despite the structural and functional similarity, very few targeted studies are available in the literature. The present review provides an overview of the role of SAR in skeletal muscle physiology, as well as of its possible involvement and dysfunction in muscle wasting disorders, in order to summarize the current knowledge on SAR and drive attention to this important but still underinvestigated/neglected protein. Full article
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