Key result
Sarcoplasmic reticulum Ca2+-ATPase from rabbit skeletal muscle forms high molecular weight complexes, estimated to be dimers and tetramers, in native membranes.
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May inform SERCA oligomer models in muscle; hypothesis-generating for cardiac Ca2+ regulation studies.
Although the primary structure and catalytic cycle of the sarcoplasmic reticulum Ca2+-ATPase has been revealed, it is not well understood whether functional Ca2+ pump proteins exist in a monomeric or an oligomeric state in native skeletal muscle membranes. Here, we show that the Ca2+-ATPase tends to form high molecular weight complexes, estimated to be dimers and tetramers using immunoblotting of two-dimensionally separated microsomal membranes following crosslinking. This agrees with both electron microscopical and biochemical findings which demonstrate that Ca2+-ATPase clusters are the predominant molecular species in native membranes and that oligomerization may play a role in cooperative kinetics and enzyme stabilization.
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Maguire et al. (1996) studied this question. Sarcoplasmic reticulum Ca2+-ATPase from rabbit skeletal muscle forms high molecular weight complexes, estimated to be dimers and tetramers, in native membranes.
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