The dimeric form of Ca super(2+)-ATPase is involved in Ca super(2+) transport in the sarcoplasmic reticulum
To identify the functional unit of Ca super(2+)-ATPase in the sarcoplasmic reticulum, we assessed Ca super(2+)-transport activities occurring on sarcoplasmic reticulum membranes with different combinations of active and inactive Ca super(2+)-ATPase molecules. We prepared heterodimers, consisting of...
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Veröffentlicht in: | Biochemical journal 2008-09, Vol.414 (Pt3), p.357-361 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | To identify the functional unit of Ca super(2+)-ATPase in the sarcoplasmic reticulum, we assessed Ca super(2+)-transport activities occurring on sarcoplasmic reticulum membranes with different combinations of active and inactive Ca super(2+)-ATPase molecules. We prepared heterodimers, consisting of a native Ca super(2+)-ATPase molecule and a Ca super(2+)-ATPase molecule inactivated by FITC labelling, by fusing vesicles loaded with each type of Ca super(2+)-ATPase. The heterodimers exhibited neither Ca super(2+) transport nor ATP hydrolysis, suggesting that Ca super(2+) transport by the Ca super(2+)-ATPase requires an interaction between functional Ca super(2+)-ATPase monomers. This finding implies that the functional unit of the Ca super(2+)-ATPase is a dimer. |
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ISSN: | 0264-6021 1470-8728 |