Chronic reduction of store operated Ca entry is viable therapeutically but is associated with cardiovascular complications.

Loss of function mutations in store-operated Ca entry (SOCE) are associated with severe paediatric disorders in humans, including combined immunodeficiency, anaemia, thrombocytopenia, anhidrosis and muscle hypotonia. Given its central role in immune cell activation, SOCE has been a therapeutic target for autoimmune and inflammatory diseases. Treatment for such chronic diseases would require prolonged SOCE inhibition.

Phosphorylation of STIM1 at ERK/CDK sites is dispensable for cell migration and ER partitioning in mitosis.

Store-operated Ca entry (SOCE) is a ubiquitous Ca influx pathway required for multiple physiological functions including cell motility. SOCE is triggered in response to depletion of intracellular Ca stores following the activation of the endoplasmic reticulum (ER) Ca sensor STIM1, which recruits the plasma membrane (PM) Ca channel Orai1 at ER-PM junctions. STIM1 is phosphorylated dynamically, and this phosphorylation has been implicated in several processes including SOCE inactivation during M-phase, maximal SOCE activation, ER segregation during mitosis, and cell migration.

The carboxy terminal coiled-coil modulates Orai1 internalization during meiosis.

Regulation of Ca signaling is critical for the progression of cell division, especially during meiosis to prepare the egg for fertilization. The primary Ca influx pathway in oocytes is Store-Operated Ca Entry (SOCE). SOCE is tightly regulated during meiosis, including internalization of the SOCE channel, Orai1.

miRNA-dependent regulation of STIM1 expression in breast cancer.

Store-operated Ca entry (SOCE) has been shown to be important for breast cancer metastasis in xenograft mouse models. The ER Ca sensor STIM1 and Orai plasma membrane Ca channels molecularly mediate SOCE. Here we investigate the role of the microRNA machinery in regulating STIM1 expression.

Remodeling of ER-plasma membrane contact sites but not STIM1 phosphorylation inhibits Ca influx in mitosis.

Store-operated Ca entry (SOCE), mediated by the endoplasmic reticulum (ER) Ca sensor stromal interaction molecule 1 (STIM1) and the plasma membrane (PM) channel Orai1, is inhibited during mitosis. STIM1 phosphorylation has been suggested to mediate this inhibition, but it is unclear whether additional pathways are involved. Here, we demonstrate using various approaches, including a nonphosphorylatable STIM1 knock-in mouse, that STIM1 phosphorylation is not required for SOCE inhibition in mitosis.