Control of STIM and Orai function by post-translational modifications
Jinsy Johnson1, Rachel Blackman1, Scott Gross1
1Fels Institute for Cancer Research and Molecular Biology Philadelphia, PA, 19140, USA.
Cell Calcium
|February 12, 2022
Summary
Post-translational modifications regulate store-operated calcium entry (SOCE) by affecting STIM and Orai proteins. This review details how phosphorylation, glycosylation, and redox changes impact SOCE key events.
Area of Science:
- Cellular Biology
- Biochemistry
- Physiology
Background:
- Store-operated calcium entry (SOCE) is crucial for cellular calcium homeostasis.
- SOCE is primarily mediated by stromal interaction molecules (STIM1/2) and Orai channels (Orai1-3).
- While ER calcium levels are primary regulators, post-translational modifications (PTMs) also significantly influence SOCE components.
Purpose of the Study:
- To review the impact of PTMs on STIM and Orai proteins.
- To elucidate how PTMs modulate critical steps in the SOCE pathway.
- To highlight the roles of phosphorylation, glycosylation, and redox modifications in SOCE regulation.
Main Methods:
- Literature review focusing on post-translational modifications.
- Analysis of studies investigating STIM and Orai protein regulation.
- Synthesis of findings on phosphorylation, glycosylation, and redox effects on SOCE.
Main Results:
- PTMs, including phosphorylation, glycosylation, and redox modifications, alter STIM and Orai functions.
- These modifications impact calcium sensing by STIM proteins.
- PTMs influence STIM translocation, Orai interaction, and Orai1 channel activation.
Conclusions:
- PTMs are critical regulators of store-operated calcium entry.
- Understanding PTMs provides deeper insights into SOCE mechanisms.
- Targeting PTMs may offer therapeutic strategies for calcium-related disorders.
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