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Related Experiment Video

Updated: Jun 15, 2026

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

Dissection of Local Ca²⁺ Signals in Cultured Cells by Membrane-targeted Ca²⁺ Indicators

Published on: March 22, 2019

Ca2+ signaling and STIM1.

Tomohiro Kurosaki¹, Yoshihiro Baba

¹Laboratory for Lymphocyte Differentiation, WPI Immunology Frontier Research Center, Osaka University, Japan. kurosaki@rcai.riken.jp

Progress in Biophysics and Molecular Biology

|March 16, 2010

Summary

Stromal interaction molecule 1 (STIM1) regulates store-operated calcium entry (SOCE), crucial for sustained intracellular calcium levels. This mechanism is vital for cell functions and allergic responses.

Area of Science:

Cell Biology
Molecular Biology
Immunology

Background:

Intracellular calcium ion concentration ([Ca(2+)]) regulates critical cell functions like adhesion, motility, gene expression, and proliferation.
The endoplasmic reticulum (ER) initially releases Ca(2+), but sustained elevation requires continuous extracellular Ca(2+) influx via store-operated Ca(2+) entry (SOCE).

Purpose of the Study:

To review the mechanism by which STIM1 regulates SOCE.
To elucidate the role of STIM1 in mast cell functions and allergic responses.

Main Methods:

The review summarizes existing research on STIM1's function in calcium signaling.
Focuses on STIM1's role in sensing ER calcium levels and activating plasma membrane calcium channels.

Main Results:

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STIM1 senses ER calcium depletion through its EF-hand domain, leading to STIM1 clustering near the plasma membrane.
Clustered STIM1 activates store-operated calcium channels, facilitating continuous extracellular calcium influx.
STIM1 plays a significant role in regulating mast cell functions and allergic responses.

Conclusions:

STIM1 is essential for maintaining intracellular calcium homeostasis through SOCE.
Understanding STIM1's mechanism provides insights into cellular regulation and allergic reactions.