The dimeric form of Ca2+-ATPase is involved in Ca2+ transport in the sarcoplasmic reticulum

Author:

Ushimaru Makoto1,Fukushima Yoshihiro1

Affiliation:

1. Department of Chemistry, Kyorin University School of Medicine, Shinkawa 6-20-2, Mitaka, Tokyo, Japan

Abstract

To identify the functional unit of Ca2+-ATPase in the sarcoplasmic reticulum, we assessed Ca2+-transport activities occurring on sarcoplasmic reticulum membranes with different combinations of active and inactive Ca2+-ATPase molecules. We prepared heterodimers, consisting of a native Ca2+-ATPase molecule and a Ca2+-ATPase molecule inactivated by FITC labelling, by fusing vesicles loaded with each type of Ca2+-ATPase. The heterodimers exhibited neither Ca2+ transport nor ATP hydrolysis, suggesting that Ca2+ transport by the Ca2+-ATPase requires an interaction between functional Ca2+-ATPase monomers. This finding implies that the functional unit of the Ca2+-ATPase is a dimer.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference25 articles.

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2. Monomer-oligomer equilibrium of sarcoplasmic reticulum Ca-ATPase and the role of subunit interaction in the Ca2+ pump mechanism;Andersen;Biochim. Biophys. Acta,1989

3. Structural basis of ion pumping by Ca2+-ATPase of the sarcoplasmic reticulum;Toyosima;Annu. Rev. Biochem.,2004

4. Determination and functional significance of low affinity nucleotide sites of Ca2+ + Mg2+ -dependent ATPase of sarcoplasmic reticulum;Eckert;Acta Biol. Med. Ger.,1977

5. Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca2+ -dependent adenosine triphosphatase of sarcoplasmic reticulum;Mitchinson;FEBS Lett.,1982

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