Binding of the second messenger inositol 1,4,5-trisphosphate to its intracellular receptor drives interaction between the intracellular Ca2+ sensor STIM and the plasma membrane localized Ca2+ channel Orai and raises the level of store-operated Ca2+ entry in mammalian cells.

Cell-wide Ca²⁺ signals that regulate numerous cellular functions comprise dual Ca²⁺ release modes through IP₃ receptors, punctate transients mediated by clustered receptors and spatiotemporally diffuse release through functionally distinct receptors.

The endoplasmic reticulum serves as a direct and primary source of calcium ions for the lysosome.

When non-glycosylated, Seipin, which spans the endoplasmic reticulum (ER) membrane twice, forms aggregates in an oligomerization-dependent manner, distorts the shape of the ER, and incorporates SERCA2b via direct interaction, inactivation of which results in induction of ER stress and apoptosis.

In a mouse model of Sjogren's disease, mitochondrial function and Ca²⁺ signaling are disrupted resulting in altered coupling between Ca²⁺ release and Ca²⁺ activated Cl^- channels and salivary gland hypofunction.

Astrocytes regulate the pruning of excitatory synapses during early life through ATP signaling.

Signaling at the primary cilium is important to sustain the morphology, connectivity, and survival of a key neural population within the brain.

Measurement of physiological intracellular Ca²⁺ signals following neural stimulation in vivo reveals distinct spatiotemporal characteristics that promote optimal salivary gland fluid secretion.

MET acts as a dependence receptor in vivo by promoting hepatocyte apoptosis, a response induced by a caspase generated fragment able to favor calcium exchange between endoplasmic reticulum and mitochondria.

Store operated calcium entry is defective in hepatocytes of obese mice, and restoring this process is sufficient to improve glucose metabolism.