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Originally published In Press as doi:10.1074/jbc.M008778200 on February 13, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16356-16364, May 11, 2001
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Structural and Functional Features of the Transmembrane Domain of the Na,K-ATPase beta  Subunit Revealed by Tryptophan Scanning*

Udo Hasler, Gilles Crambert, Jean-Daniel Horisberger, and Käthi GeeringDagger

From the Institut de Pharmacologie et Toxicologie de l'Université, rue du Bugnon 27, CH 1005-Lausanne, Switzerland

In oligomeric P2-ATPases such as Na,K- and H,K-ATPases, beta  subunits play a fundamental role in the structural and functional maturation of the catalytic alpha  subunit. In the present study we performed a tryptophan scanning analysis on the transmembrane alpha -helix of the Na,K-ATPase beta 1 subunit to investigate its role in the stabilization of the alpha  subunit, the endoplasmic reticulum exit of alpha -beta complexes, and the acquisition of functional properties of the Na,K-ATPase. Single or multiple tryptophan substitutions in the beta  subunits transmembrane domain had no significant effect on the structural maturation of alpha  subunits expressed in Xenopus oocytes nor on the level of expression of functional Na,K pumps at the cell surface. Furthermore, tryptophan substitutions in regions of the transmembrane alpha -helix containing two GXXXG transmembrane helix interaction motifs or a cysteine residue, which can be cross-linked to transmembrane helix M8 of the alpha  subunit, had no effect on the apparent K+ affinity of Na,K-ATPase. On the other hand, substitutions by tryptophan, serine, alanine, or cysteine, but not by phenylalanine of two highly conserved tyrosine residues, Tyr40 and Tyr44, on another face of the transmembrane helix, perturb the transport kinetics of Na,K pumps in an additive way. These results indicate that at least two faces of the beta  subunits transmembrane helix contribute to inter- or intrasubunit interactions and that two tyrosine residues aligned in the beta  subunits transmembrane alpha -helix are determinants of intrinsic transport characteristics of Na,K-ATPase.

* This work was supported by Swiss National Fund for Scientific Research Grant 31-53721.98.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Institut de Pharmacologie et de Toxicologie, rue du Bugnon 27, CH-1005 Lausanne, Switzerland. Tel.: 41-21-692-54-10; Fax: 41-21-692-53-55; E-mail: kaethi.geering@ipharm.unil.ch.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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