Ca2+ mobilization in response to cross-linking of IgE bound to its high affinity receptor, FcεRI, on mast cells is central to immune allergic responses. Stimulated tyrosine phosphorylation caused by this cross-linking activates store-operated Ca2+ entry that results in sustained Ca2+ oscillations dependent on Rho family GTPases and phosphoinositide synthesis. Coupling of the endoplasmic reticulum (ER) Ca2+ sensor, stromal interaction molecule 1 (STIM1), to the Ca2+-selective channel, Orai1, is regulated by these elements and depends on membrane organization, both at the plasma membrane and at the ER. Mitochondria also contribute to the regulation of Ca2+ mobilization, and we describe recent evidence that the ER membrane protein vesicle-associated membrane protein-associated protein (VAP) plays a significant role in the coupling between ER and mitochondria in this process. In addition to granule exocytosis, Ca2+ mobilization in these cells also contributes to stimulated outward trafficking of recycling endosomes and to antigen-stimulated chemotaxis, and it is pathologically regulated by protozoan parasitic invasion.
Roles for Ca2+ mobilization and its regulation in mast cell functions: recent progress
- Views Icon Views
- Share Icon Share
David Holowka, Marcus Wilkes, Christopher Stefan, Barbara Baird; Roles for Ca2+ mobilization and its regulation in mast cell functions: recent progress. Biochem Soc Trans 15 April 2016; 44 (2): 505–509. doi: https://doi.org/10.1042/BST20150273
Download citation file: