Abstract
Na,K-ATPase, an essential transporter of mammalian cells, is an oligomeric transmembrane protein composed of two subunits, alpha and beta, of which there are several isoforms. In this study, we demonstrate that the alpha1 and alpha2 isoforms of the Na,K-ATPase alpha subunit are modified by the covalent attachment of ubiquitin polymers in COS-7 cells. We propose that polyubiquitination of the Na,K-ATPase alpha subunit may play a role in regulating its degradation.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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COS Cells
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Cell Membrane / enzymology
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Cysteine Endopeptidases / metabolism
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Multienzyme Complexes / metabolism
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Proteasome Endopeptidase Complex
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Protein Processing, Post-Translational
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Sodium-Potassium-Exchanging ATPase / metabolism*
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Ubiquitins / metabolism*
Substances
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Multienzyme Complexes
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Ubiquitins
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Sodium-Potassium-Exchanging ATPase