Role of the transmembrane and extracytoplasmic domain of beta subunits in subunit assembly, intracellular transport, and functional expression of Na,K-pumps.

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Serval ID
serval:BIB_EE9F0801F9FD
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Role of the transmembrane and extracytoplasmic domain of beta subunits in subunit assembly, intracellular transport, and functional expression of Na,K-pumps.
Journal
The Journal of cell biology
Author(s)
Jaunin P., Jaisser F., Beggah A.T., Takeyasu K., Mangeat P., Rossier B.C., Horisberger J.D., Geering K.
ISSN
0021-9525
ISSN-L
0021-9525
Publication state
Published
Issued date
12/1993
Peer-reviewed
Oui
Volume
123
Number
6 Pt 2
Pages
1751-1759
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Abstract
The ubiquitous Na,K- and the gastric H,K-pumps are heterodimeric plasma membrane proteins composed of an alpha and a beta subunit. The H,K-ATPase beta subunit (beta HK) can partially act as a surrogate for the Na,K-ATPase beta subunit (beta NK) in the formation of functional Na,K-pumps (Horisberger et al., 1991. J. Biol. Chem. 257:10338-10343). We have examined the role of the transmembrane and/or the ectodomain of beta NK in (a) its ER retention in the absence of concomitant synthesis of Na,K-ATPase alpha subunits (alpha NK) and (b) the functional expression of Na,K-pumps at the cell surface and their activation by external K+. We have constructed chimeric proteins between Xenopus beta NK and rabbit beta HK by exchanging their NH2-terminal plus transmembrane domain with their COOH-terminal ectodomain (beta NK/HK, beta HK/NK). We have expressed these constructs with or without coexpression of alpha NK in the Xenopus oocyte. In the absence of alpha NK, Xenopus beta NK and all chimera that contained the ectodomain of beta NK were retained in the ER while beta HK and all chimera with the ectodomain of beta HK could leave the ER suggesting that ER retention of unassembled Xenopus beta NK is mediated by a retention signal in the ectodomain. When coexpressed with alpha NK, only beta NK and beta NK/HK chimera assembled efficiently with alpha NK leading to similar high expression of functional Na,K-pumps at the cell surface that exhibited, however, a different apparent K+ affinity. beta HK or chimera with the transmembrane domain of beta HK assembled less efficiently with alpha NK leading to lower expression of functional Na,K-pumps with a different apparent K+ affinity. The data indicate that the transmembrane domain of beta NK is important for efficient assembly with alpha NK and that both the transmembrane and the ectodomain of beta subunits play a role in modulating the transport activity of Na,K-pumps.
Keywords
Amino Acid Sequence, Animals, Base Sequence, Cell Membrane/enzymology, Female, Gastric Mucosa/enzymology, Gene Expression, H(+)-K(+)-Exchanging ATPase/biosynthesis, H(+)-K(+)-Exchanging ATPase/metabolism, Macromolecular Substances, Molecular Sequence Data, Oocytes/physiology, Polymerase Chain Reaction, Protein Biosynthesis, Protein Processing, Post-Translational, Rabbits, Recombinant Fusion Proteins/biosynthesis, Recombinant Fusion Proteins/metabolism, Sodium-Potassium-Exchanging ATPase/biosynthesis, Sodium-Potassium-Exchanging ATPase/metabolism, Xenopus laevis
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 13:28
Last modification date
09/08/2024 15:53
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