Holowka, D; Wilkes, M; Stefan, C; Baird, B; (2016) Roles for Ca2+ mobilization and its regulation in mast cell functions: recent progress. Biochemical Society Transactions , 44 (2) pp. 505-509. 10.1042/BST20150273.

Preview

Text Stefan_Holowka_BiochemSocTrans_revrefs-f.pdf Download (1MB) | Preview

Abstract

Ca(2+)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 Ca(2+)entry that results in sustained Ca(2+)oscillations dependent on Rho family GTPases and phosphoinositide synthesis. Coupling of the endoplasmic reticulum (ER) Ca(2+)sensor, stromal interaction molecule 1 (STIM1), to the Ca(2+)-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 Ca(2+)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, Ca(2+)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.

Download activity - last month

Export as CSVJSONXML

Download activity - last 12 months

Export as CSVXMLJSON

Downloads by country - last 12 months

Export as CSVJSONXML

Archive Staff Only

View Item