STIM proteins: dynamic calcium signal transducers
By J. Soboloff, B. S. Rothberg, M. Madesh, D. Gill. Nature reviews. Molecular cell biology, 2012
650 citations recorded by the source corpus.
Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca2+) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca2+ stored within the ER lumen. As ER Ca2+ is released to generate primary Ca2+ signals, STIM proteins undergo an intricate activation reaction and rapidly translocate into junctions formed between the ER and the plasma membrane. There, STIM proteins tether and activate the highly Ca2+-selective Orai channels to mediate finely controlled Ca2+ signals and to homeostatically balance cellular Ca2+. Details are emerging on the remarkable organization within these STIM-induced junctional microdomains and the identification of new regulators and alternative target proteins for STIM.
Subfields: Biochemistry, Immunology, Sensory Systems
View Paper: https://www.semanticscholar.org/paper/154ca063518b9195c1c108a14488b7cb9be6a85b
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Citations in the corpus
- Handbook of ion channels (2015, background): “However, recent evidence reveals fascinating differences in the behavior of these proteins from those of canonical CRAC channels, including but not limited to store-independent regulation and altered ion conduction properties [106,136].”
- Initiation and perpetuation of NLRP3 inflammasome activation and assembly (2015, background): “SOCE (or calcium release-activated channels) respond to transient increases in cytosolic Ca by permitting additional extracellular Ca influx, and include channel-forming proteins ORAI1, ORAI2, and ORAI3 and sensor proteins STIM1 and STIM2 (87, 88).”