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Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis

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Bioscience Reports

Abstract

The results of site-directed mutagenesis studies of the sarcoplasmic reticulum Ca2+-ATPase are reviewed. More than 250 different point mutants have been expressed in cell culture and analysed by a panel of functional assays. Thereby, 40–50 important amino acid residues have been pinpointed, and the mutants have been assigned to functional classes: the Ca2+-affinity mutants, the phosphorylation-negative mutants, the ATP-affinity mutants, the E1P mutants, the E2P mutants, and the uncoupled mutants. Moreover, regions important to the specific inhibition by thapsigargin have been identified by analysis of Ca2+-ATPase/Na+, K+-ATPase chimeric constructs.

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  1. Department of Physiology, University of Aarhus, Ole Worms Allé 160, DK-8000, Aarhus C, Denmark

    Jens Peter Andersen

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Andersen, J.P. Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis. Biosci Rep 15, 243–261 (1995). https://doi.org/10.1007/BF01788358

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