期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 365, 期 3, 页码 706-714出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.10.029
关键词
transmembrane domain; heptad repeat motif; GxxxG; glycine zipper; Na,K-ATPase
资金
- NIDDK NIH HHS [R01 DK056216, DK 56216] Funding Source: Medline
- NIGMS NIH HHS [R01 GM063919, R01 GM063919-08, R01 GM063919-05, R01 GM063919-07, R01 GM063919-04, R01 GM063919-06] Funding Source: Medline
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.
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