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Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Maintaining cellular homeostasis is vital for organism health. Disrupted endoplasmic reticulum (ER) calcium (Ca2+) signaling and homeostasis activate the unfolded protein response (UPR) to cope with cellular stress.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Physiology

Background:

  • Cellular homeostasis is essential for organismal health.
  • Disruptions in homeostasis trigger cellular stress responses, notably the unfolded protein response (UPR) mediated by IRE1α, PERK, and ATF6.
  • Calcium (Ca2+) signaling is integral to stress responses, with the endoplasmic reticulum (ER) serving as a primary Ca2+ storage and signaling source.

Purpose of the Study:

  • To investigate the role of ER Ca2+ homeostasis in activating ER stress coping mechanisms.
  • To explore the interplay between ER Ca2+ dynamics and the unfolded protein response (UPR).

Main Methods:

  • Focus on selected aspects of ER Ca2+ homeostasis.
  • Analysis of proteins involved in ER Ca2+ transport and storage.
  • Examination of ER Ca2+ stores refilling mechanisms.

Main Results:

  • ER Ca2+ homeostasis is a key factor in regulating ER stress.
  • Specific proteins within the ER manage Ca2+ flux, influencing cellular stress signaling.
  • ER Ca2+ refilling processes are critical for maintaining cellular balance under stress.

Conclusions:

  • ER Ca2+ homeostasis is intrinsically linked to the activation and regulation of ER stress responses like the UPR.
  • Understanding ER Ca2+ dynamics provides insights into cellular adaptation to stress.
  • Targeting ER Ca2+ signaling pathways may offer therapeutic strategies for stress-related disorders.