title: Dissecting ICRAC, a store-operated calcium current.
abstract: The use of Ca(2+) for intracellular signalling necessitates tight local and global control of cytoplasmic Ca(2+) concentration, and mechanisms for maintaining the net Ca(2+) balance. It has long been recognized that intracellular Ca(2+) stores exert control over Ca(2+) influx at the plasma membrane through a process of store-operated Ca(2+) entry (SOCE). The Ca(2+) current I(CRAC) is the best characterized instance of SOCE, but the elements of the pathway leading to I(CRAC) have eluded biochemical definition for more than a decade. However, the recent identification of key proteins underlying I(CRAC)--STIM1 and Orai1--has led to several insights into this ER-to-plasma membrane signalling system and to the recognition that it is an ancient and conserved mechanism in multicellular organisms.
authors: The CBR Institute for Biomedical Research, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA. hogan@cbr.med.harvard.edu <hogan@cbr.med.harvard.edu>
authors: Patrick G
authors: PG
authors: Hogan
authors: Anjana
authors: A
authors: Rao
mesh_terms: D000818:Animals; D001692:Biological Transport / Q000502:physiology; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000502:physiology*; D020013:Calcium Signaling / Q000502:physiology*; D006801:Humans; D008954:Models, Biological
chemical_list: D015220:Calcium Channels; D002118:Calcium