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Updated: Jun 20, 2026
10:45
Isolation of Human Myoblasts, Assessment of Myogenic Differentiation, and Store-operated Calcium Entry Measurement
Published on: July 26, 2017
Recent progress on STIM1 domains controlling Orai activation
1Institute of Biophysics, University of Linz, A-4040 Linz, Austria. rainer.schindl@jku.at
Cell Calcium
|September 8, 2009
Summary
Store-operated calcium entry in non-excitable cells relies on STIM1 and Orai1. Recent research focuses on STIM1
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- Store-operated calcium (Ca2+) entry is crucial for non-excitable cells.
- The CRAC channel, comprising STIM1 and Orai1, mediates this process.
- STIM1 (stromal interaction molecule 1) senses ER Ca2+ depletion and interacts with Orai1 (calcium release-activated calcium channel protein 1) in the plasma membrane to activate Ca2+ influx.
Purpose of the Study:
- To review recent advancements in understanding the molecular mechanisms of STIM1-Orai1 interaction.
- To highlight specific domains within the cytosolic part of STIM1 that regulate this crucial coupling.
Main Methods:
- Literature review of recent studies on STIM1 and Orai1.
- Analysis of domain interactions within the STIM1 protein.
Main Results:
- The STIM1-Orai1 interaction is primarily mediated through their C-terminal regions.
- Specific domains within the cytosolic portion of STIM1 are critical for governing the coupling and activation of Orai1 channels.
- Recent findings shed light on the structural and functional significance of these STIM1 domains.
Conclusions:
- Understanding the STIM1-Orai1 interaction domains is key to elucidating store-operated calcium entry.
- This knowledge may pave the way for therapeutic interventions targeting calcium signaling pathways.
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