By restricting actin polymerization to the perimeter of the immune synapse and promoting depolymerization, calcium influx drives centripetal actin flow, which confines CRAC channels and the endoplasmic reticulum to the synapse center.
VRAC activation, observed with a FRET sensor of intracellular LRRC8-domains movement during gating and by fluorometry, requires plasma membrane localization and diacylglycerol signaling, but is independent of intracellular ionic strength.
The conserved biochemical activity of the duplicate Bab transcription factors were integrated into the regulatory hierarchy of an evolving gene regulatory network by binding site gains in a target gene's cis-regulatory region.
The activation and membrane localization of the broadly-tuned noxious chemosensory cation channel TRPA1 are regulated by direct interactions with cholesterol via CRAC motifs in transmembane segments 2 and 4.
LRRC8A is an essential component of a mechanoresponsive ion channel signaling complex that tunes skeletal muscle differentiation, muscle cell size, function and metabolic pathways to regulate adiposity and systemic glycemia.
Electrophysiological and molecular modeling studies identify a sulfur-aromatic interaction between the hydrophobic channel gate and a nearby methionine residue, termed the "gate latch", which is essential for Orai1 pore opening.