NDLI: Structure and Functional Analysis of a $Ca^{2+}$ Sensor Mutant of the $Na^{+}/Ca^{2+}$ Exchanger

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Structure and Functional Analysis of a $Ca^{2+}$ Sensor Mutant of the $Na^{+}/Ca^{2+}$ Exchanger

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Structure and Functional Analysis of a $Ca^{2+}$ Sensor Mutant of the $Na^{+}/Ca^{2+}$ Exchanger

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mercado-besserer, Gabriel Ottolia, Michela Chaptal, Vincent Philipson, Kenneth D. Nicoll, Debora A. Abramson, Jeff
Description	Author Affiliation: Chaptal V ( Department of Physiology and Cardiovascular Research Laboratories, David Geffen School of Medicine at UCLA, Los Angeles, California 90095, USA.)
Abstract	The mammalian Na(+)/Ca(2+) exchanger, NCX1.1, serves as the main mechanism for Ca(2+) efflux across the sarcolemma following cardiac contraction. In addition to transporting Ca(2+), NCX1.1 activity is also strongly regulated by Ca(2+) binding to two intracellular regulatory domains, CBD1 and CBD2. The structures of both of these domains have been solved by NMR spectroscopy and x-ray crystallography, greatly enhancing our understanding of Ca(2+) regulation. Nevertheless, the mechanisms by which Ca(2+) regulates the exchanger remain incompletely understood. The initial NMR study showed that the first regulatory domain, CBD1, unfolds in the absence of regulatory Ca(2+). It was further demonstrated that a mutation of an acidic residue involved in Ca(2+) binding, E454K, prevents this structural unfolding. A contradictory result was recently obtained in a second NMR study in which Ca(2+) removal merely triggered local rearrangements of CBD1. To address this issue, we solved the crystal structure of the E454K-CBD1 mutant and performed electrophysiological analyses of the full-length exchanger with mutations at position 454. We show that the lysine substitution replaces the Ca(2+) ion at position 1 of the CBD1 Ca(2+) binding site and participates in a charge compensation mechanism. Electrophysiological analyses show that mutations of residue Glu-454 have no impact on Ca(2+) regulation of NCX1.1. Together, structural and mutational analyses indicate that only two of the four Ca(2+) ions that bind to CBD1 are important for regulating exchanger activity.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	22
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-05-29
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Metabolism Mutation Genetics Sodium-Calcium Exchanger Chemistry Animals Binding Sites Conserved Sequence DNA Mutational Analysis Protein Structure, Secondary Protein Structure, Tertiary Structure-Activity Relationship Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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