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Structural elements of stromal interaction molecule function.
Matthew J Novello1, Jinhui Zhu1, Qingping Feng1
1Department of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada.
Cell Calcium
|April 27, 2018
Summary
Stromal interaction molecules (STIMs) sense calcium levels and signal to Orai1 channels. Structural data reveals key interactions driving STIM activation and Orai1 channel function.
Area of Science:
- Molecular biology
- Cellular signaling
- Structural biology
Background:
- Stromal interaction molecules (STIM)-1 and -2 are key regulators of store-operated calcium entry.
- STIM proteins sense intracellular calcium levels and activate Orai1 channels.
Purpose of the Study:
- To review high-resolution structural data on STIM proteins.
- To elucidate the molecular mechanisms of STIM-mediated Orai1 channel activation.
Main Methods:
- X-ray crystallography
- Solution Nuclear Magnetic Resonance (NMR) spectroscopy
- Structural analysis of protein-protein interactions
Main Results:
- High-resolution structures reveal intramolecular and intermolecular interactions critical for STIM activation.
- Specific EF-hand, sterile α motif, and coiled-coil interactions are key to STIM function.
- Post-translational modifications impact STIM structure and function.
Conclusions:
- Structural insights are crucial for understanding STIM-Orai1 channel regulation.
- Further studies on STIM:Orai complexes are needed to fully define activation mechanisms.
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