STIM family of proteins
Ritchie, Michael F. Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania.
Soboloff, Jonathan Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania.
- Critical biological functions for STIM proteins
- Links to Primary Literature
- Additional Readings
Calcium (Ca2+) is a major signaling molecule that activates an array of cellular events. Accordingly, cytosolic Ca2+ levels are tightly controlled at approximately 100 nM. However, elevations to approximately 300 nM initiate powerful signals that control a spectrum of cell functions, ranging from short-term contractile responses to long-term events such as transcription. Thus, maintenance of cytosolic Ca2+ is a very important and elaborate process. Some of the regulatory elements that maintain these cytosolic Ca2+ levels are ion channels and exchangers located on the plasma membrane of the cell. However, the endoplasmic reticulum (ER) also plays a large role in Ca2+ signaling. The ER lumen stores approximately 500 μM of Ca2+, which not only provides an environment conducive for proper protein folding, but also serves as a major source of Ca2+ for signaling.
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