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| Content Provider | Springer Nature Link |
|---|---|
| Author | Morrill, Gene A. Kostellow, Adele B. Liu, Lijun Gupta, Raj K. Askari, Amir |
| Copyright Year | 2016 |
| Abstract | Na/K-ATPase is a key plasma membrane enzyme involved in cell signaling, volume regulation, and maintenance of electrochemical gradients. The α-subunit, central to these functions, belongs to a large family of P-type ATPases. Differences in transmembrane (TM) helix topology, sequence homology, helix–helix contacts, cell signaling, and protein domains of Na/K-ATPase α-subunit were compared in fungi (Beauveria), unicellular organisms (Paramecia), primitive multicellular organisms (Hydra), and vertebrates (Xenopus, Homo sapiens), and correlated with evolution of physiological functions in the α-subunit. All α-subunits are of similar length, with groupings of four and six helices in the N- and C-terminal regions, respectively. Minimal homology was seen for protein domain patterns in Paramecium and Hydra, with high correlation between Hydra and vertebrates. Paramecium α-subunits display extensive disorder, with minimal helix contacts. Increases in helix contacts in Hydra approached vertebrates. Protein motifs known to be associated with membrane lipid rafts and cell signaling reveal significant positional shifts between Paramecium and Hydra vulgaris, indicating that regional membrane fluidity changes occur during evolution. Putative steroid binding sites overlapping TM-3 occurred in all species. Sites associated with G-protein-receptor stimulation occur both in vertebrates and amphibia but not in Hydra or Paramecia. The C-terminus moiety “KETYY,” necessary for the Na+ activation of pump phosphorylation, is not present in unicellular species indicating the absence of classical Na+/K+-pumps. The basic protein topology evolved earliest, followed by increases in protein domains and ordered helical arrays, correlated with appearance of α-subunit regions known to involve cell signaling, membrane recycling, and ion channel formation. |
| Starting Page | 183 |
| Ending Page | 198 |
| Page Count | 16 |
| File Format | |
| ISSN | 00222844 |
| Journal | Journal of Molecular Evolution |
| Volume Number | 82 |
| Issue Number | 4-5 |
| e-ISSN | 14321432 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2016-03-10 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Na/K-ATPase α-subunit Evolution Protein domains Transmembrane helix Cell signaling Helix–helix interactions Evolutionary Biology Microbiology Plant Sciences Plant Genetics & Genomics Animal Genetics and Genomics Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Molecular Biology Ecology, Evolution, Behavior and Systematics |
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