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ATP Driven Pumps II: P-type Pumps01:34

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Related Experiment Video

Updated: May 23, 2026

Fluorescence-based Measurement of Store-operated Calcium Entry in Live Cells: from Cultured Cancer Cell to Skeletal Muscle Fiber
14:18

Fluorescence-based Measurement of Store-operated Calcium Entry in Live Cells: from Cultured Cancer Cell to Skeletal Muscle Fiber

Published on: February 13, 2012

Store-operated Ca(2+) entry.

Alejandro Berna-Erro1, Pedro C Redondo, Juan A Rosado

  • 1Department of Physiology, Cell Physiology Research Group, University of Extremadura, Cáceres 10003, Spain.

Advances in Experimental Medicine and Biology
|March 29, 2012
PubMed
Summary
This summary is machine-generated.

Store-operated calcium entry (SOCE) involves STIM1 and Orai1 proteins sensing and conducting calcium influx. These proteins, along with TRPC channels, form dynamic complexes that explain varied calcium currents in cells.

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Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels
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Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels

Published on: December 13, 2024

Area of Science:

  • Cell Biology
  • Physiology
  • Molecular Biology

Background:

  • Store-operated calcium entry (SOCE) is a fundamental mechanism for calcium influx in mammalian cells.
  • The precise mechanisms of calcium store communication and the nature of capacitative channels have been extensively studied since 1986.

Purpose of the Study:

  • To elucidate the molecular players and interactions governing SOCE.
  • To understand the roles of STIM, Orai, and TRPC proteins in mediating calcium entry.

Main Methods:

  • Identification and characterization of STIM and Orai proteins.
  • Investigation of protein-protein interactions using various cellular models.
  • Analysis of calcium currents (e.g., I(CRAC), I(SOC)).

Main Results:

  • STIM1 (calcium sensor) and Orai1 (calcium channel) were identified as key components of SOCE.
  • TRPC proteins were previously implicated in SOCE, potentially forming non-selective currents.
  • Evidence suggests STIM1, Orai1, and TRPC proteins form a dynamic ternary complex mediating SOCE.

Conclusions:

  • The dynamic interactions between STIM1, Orai1, and TRPC proteins provide a framework for understanding diverse SOCE currents.
  • Further characterization of STIM2, Orai2, and Orai3 roles in SOCE is warranted.