P2-type ATPases such as the plasma membrane Na+/K+-ATPase, the gastric H+/K+-ATPase and the sarcoplasmic reticulum Ca2+-ATPase are transmembrane proteins that pump metal ions across membranes. The Na+/K+-ATPase and H+/K+-ATPase each comprise a catalytic α subunit and a β subunit that is essential for correct folding. The Ca2+-ATPase has an α subunit but – despite having a topology and overall hydropathy similar to its relatives – seems to get by without a β subunit. So how can it fold correctly? Masaru Kawamura and co-workers show that it can borrow β subunits from its relatives (see p. 1875). They find that the Ca2+-ATPase can be coimmunoprecipitated with the β-subunits of the Na+/K+-ATPase and H+/K+-ATPase in oocytes during the early stages of...

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