Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/23275
Title: Ca2+ regulation in the Na+/Ca2+ exchanger involves two markedly different Ca2+ sensors.
Authors: Hilge, M
Aelen, J
Vuister, GW
First Published: 7-Apr-2006
Citation: MOL CELL, 2006, 22 (1), pp. 15-25
Abstract: The plasma membrane Na+/Ca2+ exchanger (NCX) is almost certainly the major Ca2+ extrusion mechanism in cardiac myocytes. Binding of Na+ and Ca2+ ions to its large cytosolic loop regulates ion transport of the exchanger. We determined the solution structures of two Ca2+ binding domains (CBD1 and CBD2) that, together with an alpha-catenin-like domain (CLD), form the regulatory exchanger loop. CBD1 and CBD2 are very similar in the Ca2+ bound state and describe the Calx-beta motif. Strikingly, in the absence of Ca2+, the upper half of CBD1 unfolds while CBD2 maintains its structural integrity. Together with a 7-fold higher affinity for Ca2+, this suggests that CBD1 is the primary Ca2+ sensor. Specific point mutations in either domain largely allow the interchange of their functionality and uncover the mechanism underlying Ca2+ sensing in NCX.
DOI Link: 10.1016/j.molcel.2006.03.008
ISSN: 1097-2765
Links: http://hdl.handle.net/2381/23275
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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