Abstract
Store-operated calcium (SOC) entry is essential for maintaining endoplasmic reticulum (ER) functions and generating the sustained calcium signals crucial for gene expression, secretion, cell motility, and cell proliferation. To understand the molecular mechanism of how receptor-evoked ER calcium store depletion induces calcium entry through SOC channels at the plasma membrane, we screened a small interference RNA (siRNA) library targeting the human signaling proteome and identified several regulators of SOC entry including STIM1 and STIM2.
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