The extracellular domain of the sodium pump beta isoforms determines complex stability with alpha 1

Both subunits of the Na,K-ATPase are encoded by several genes giving rise to at least six isozymes. To examine whether beta isoforms assemble with alpha 1 in a selective manner, we have overexpressed wild-type and chimeric beta subunits in L929 cells and examined assembly as a function of resistance towards detergent-mediated dissociation. In the presence of digitonin all beta chimeras coimmunoprecipitate the endogenous alpha 1 subunit. Only beta proteins with the ectodomain of beta 1 coimmunoprecipitate alpha 1 in the presence of Triton X-100. All beta chimeras stimulate Na,K-ATPase activity in L929 cells. These data indicate that the beta subunit ectodomains mediate interactions with alpha 1 and influence the stability of this complex.