Na,K-ATPase, an essential transporter of mammalian cells, is an oligom
eric transmembrane protein composed of two subunits, alpha and beta, o
f which there are several isoforms. In this study, me demonstrate that
the alpha 1 and alpha 2 isoforms of the Na,K-ATPase alpha subunit are
modified by the covalent attachment of ubiquitin polymers in COS-7 ce
lls. We propose that polyubiquitination of the Na,K-ATPase alpha subun
it may play a role in regulating its degradation. (C) 1997 Federation
of European Biochemical Societies.