Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 44, Issue -, Pages 505-509Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20150273
Keywords
calcium mobilization; IgE receptors; mast cells; mitochondrial-endoplasmic reticulum coupling; vesicle-associated membrane protein-associated protein (VAP)
Categories
Funding
- National Institutes of Health (National Institute of Allergy and Infectious Diseases) [R01 AI018306, R01 AI022499]
- MRC [MC_UU_12018/6] Funding Source: UKRI
- Medical Research Council [MC_UU_12018/6] Funding Source: researchfish
Ask authors/readers for more resources
Ca2+ mobilization in response to cross-linking of IgE bound to its high affinity receptor, Fc epsilon RI, 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available