Janus model of the Na,K-ATPase beta-subunit transmembrane domain: Distinct faces mediate alpha/beta assembly and beta-beta homo-oligomerization
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- Title
- Janus model of the Na,K-ATPase beta-subunit transmembrane domain: Distinct faces mediate alpha/beta assembly and beta-beta homo-oligomerization
- Authors
- Barwe, SP; Kim, S; Rajasekaran, SA; Bowie, JU; Rajasekaran, AK
- Date Issued
- 2007-01-19
- Publisher
- ACADEMIC PRESS LTD ELSEVIER SCIENCE L
- Abstract
- Na,K-ATPase is a hetero-oligomer of a and beta-subunits. The Na,K-ATPase beta-subunit (Na,K-beta) is involved in both the regulation of ion transport activity, and in cell-cell adhesion. By structure prediction and evolutionary analysis, we identified two distinct faces on the Na,K-beta transmembrane domain (TMD) that could mediate protein-protein interactions: a glycine zipper motif and a conserved heptad repeat. Here, we show that the heptad repeat face is involved in the hetero-oligomeric interaction of Na,K-beta with Na,K-alpha, and the glycine zipper face is involved in the homo-oligomerization of Na, K-beta. Point mutations in the heptad repeat motif reduced Na,K-beta binding to Na,K-a, and Na,K-ATPase activity. Na,K-beta TMD homo-oligomerized in biological membranes, and mutation of the glycine zipper motif affected oligomerization and cell-cell adhesion. These results provide a structural basis for understanding how Na,K-beta links ion transport and cell-cell adhesion. (c) 2006 Elsevier Ltd. All rights reserved.
- Keywords
- transmembrane domain; heptad repeat motif; GxxxG; glycine zipper; Na,K-ATPase; MEMBRANE-PROTEINS; E-CADHERIN; DIMERIZATION MOTIF; HELIX INTERACTIONS; CELL-MEMBRANES; NA+/K+-ATPASE; GXXXG MOTIF; ASSOCIATION; RESIDUES; PACKING
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/23617
- DOI
- 10.1016/j.jmb.2006.10.029
- ISSN
- 0022-2836
- Article Type
- Article
- Citation
- JOURNAL OF MOLECULAR BIOLOGY, vol. 365, no. 3, page. 706 - 714, 2007-01-19
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