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Partner of stromal interaction molecule 1 (POST), also known as SLC35G1 or TMEM20, is a 10-transmembrane-spanning protein that plays a critical role in regulating intracellular calcium homeostasis. It functions as a scaffolding molecule that, upon depletion of endoplasmic reticulum (ER) calcium stores, facilitates the binding of the ER calcium sensor STIM1 to a variety of plasma membrane and organellar transporters, including the plasma membrane Ca2+ ATPase (PMCA), the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA), and the Na+/K+-ATPase. By recruiting STIM1 to these targets, the POST complex modulates their activity—for instance, by inhibiting PMCA-mediated calcium extrusion to sustain elevated cytosolic calcium levels necessary for signaling. Beyond ion transporters, POST also associates with nuclear transport proteins like importins and exportins, suggesting a broader role in coordinating cellular responses to calcium store depletion. Given its central role in the store-operated calcium entry (SOCE) pathway, POST is a potential therapeutic target for diseases characterized by calcium dysregulation, such as certain immune disorders and cancers.
POST acts as a scaffolding protein that facilitates the interaction between STIM1 and various transporters, including PMCA, SERCA, Na+/K+-ATPase, and nuclear importins/exportins, upon endoplasmic reticulum calcium depletion to modulate calcium signaling and transport activity.
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