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J Biol Chem, Vol. 274, Issue 12, 8217-8223, March 19, 1999

beta -Subunit Assembly Is Essential for the Correct Packing and the Stable Membrane Insertion of the H,K-ATPase alpha -Subunit

Ahmed T. BeggahDagger , Pascal BéguinDagger , Krister Bamberg§, George Sachs, and Käthi GeeringDagger

From the Dagger  Institut de Pharmacologie et de Toxicologie de l'Université, Rue du Bugnon 27, CH-1005 Lausanne, Switzerland, § Astra Hässle AB, S-43183 Möldahl, Sweden, and  West Los Angeles, Wadsworth Veterans Administration-Medical Center, Los Angeles, California 90073

The alpha -subunits of H,K-ATPase (HKAalpha ) and Na,K-ATPase require a beta -subunit for maturation. We investigated the role of the beta -subunit in the membrane insertion and stability of the HKAalpha expressed in Xenopus oocytes. Individual membrane segments M1, M2, M3, M4, and M9 linked to a glycosylation reporter act as signal anchor (SA) motifs, and M10 acts as a partial stop transfer motif. In combined HKAalpha constructs, M2 acts as an efficient stop transfer sequence, and M3 acts as a SA sequence. However, M5 and M9 have only partial SA function, and M7 has no SA function. Consistent with the membrane insertion properties of segments in combined alpha  constructs, M1-3 alpha -proteins are resistant to cellular degradation, and M1-5 up to M1-10 alpha -proteins are not resistant to cellular degradation. However, co-expression with beta -subunits increases the membrane insertion of M9 in a M1-9 alpha -protein and completely protects M1-10 alpha -proteins against cellular degradation. Our results indicate that HKAalpha N-terminal (M1-M4) membrane insertion and stabilization are mediated by intrinsic molecular characteristics; however, the C-terminal (M5-M10) membrane insertion and thus the stabilization of the entire alpha -subunit depend on intramolecular and intermolecular beta -subunit interactions that are similar but not identical to data obtained for the Na,K-ATPase alpha -subunit.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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