Calcium ions have important roles in a variety of cellular processes, including intracellular signaling, protein folding, enzyme activation, and initiation of programmed cell death. Stromal interaction molecule (STIM) proteins are critical components in coordinating calcium release and entry signals and in maintaining cellular calcium homeostasis. As calcium sensors in the interior of the endoplasmic reticulum (ER), STIM proteins are activated by changes of ER calcium levels and then rapidly translocate into junctions formed between the ER and the plasma membrane, where they interact with plasma membrane ORAI channels to mediate finely controlled calcium ion signals and to homeostatically balance cellular calcium ions. New studies reveal that, besides calcium ions, STIM proteins can respond to other cellular stressors, such as oxidative and hypoxic conditions, temperature fluctuation, and changes in pH. Moreover, these proteins are also involved in some tissue-specific functions, such as growth and development of different muscles.
Dysregulation of calcium flux has been reported in cancers, autoimmune diseases, and other diseases. Thus, STIM proteins are important therapeutic targets in diseases with dysregulated calcium flux. Here, we give an introduction that briefly summarizes the role of STIM proteins as stress sensors, the molecular mechanisms, and their implications in different diseases.
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