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STIM1 regulates store-operated Ca2+ entry in oocytes
Sehwon Koh1, Kiho Lee, Chunmin Wang
1Department of Molecular Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, USA.
Developmental Biology
|April 14, 2009
Summary
Stromal interaction molecule 1 (STIM1) acts as a calcium sensor in oocytes. Upon calcium store depletion, STIM1 moves to the plasma membrane to activate calcium entry.
Area of Science:
- Cell Biology
- Molecular Biology
- Physiology
Background:
- Stromal interaction molecule 1 (STIM1) is a transmembrane protein involved in calcium signaling.
- STIM1 is proposed to sense calcium levels in the endoplasmic reticulum and regulate store-operated calcium channels.
Purpose of the Study:
- To investigate the presence, localization, and function of STIM1 in store-operated calcium entry in pig oocytes.
- To elucidate the role of STIM1 in calcium homeostasis in oocytes.
Main Methods:
- Cloning and sequence analysis of porcine STIM1.
- Immunocytochemistry and fluorescent protein tagging to determine STIM1 localization.
- Overexpression and siRNA-mediated knockdown of STIM1 to assess its function in calcium influx.
- Inhibition of store-operated calcium channels using lanthanum.
Main Results:
- Porcine STIM1 was identified, with a coding sequence of 2058 bp.
- In oocytes with replete calcium stores, STIM1 localized to the inner cytoplasm.
- Calcium store depletion induced STIM1 redistribution to the plasma membrane.
- Increased STIM1 expression enhanced calcium influx, while STIM1 knockdown abolished it.
- Lanthanum treatment inhibited the store-operated calcium influx.
Conclusions:
- STIM1 functions as a calcium sensor in pig oocytes, detecting calcium store content.
- Upon store depletion, STIM1 translocates to the plasma membrane to facilitate store-operated calcium entry.
- STIM1 plays a critical role in regulating calcium influx in oocytes.
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