Distinct pH dependencies of Na⁺/K⁺ selectivity at the two faces of Na,K-ATPase.

ABSTRACT: The sodium pump (Na,K-ATPase) in animal cells is vital for actively maintaining ATP hydrolysis-powered Na⁺ and K⁺ electrochemical gradients across the cell membrane. These ion gradients drive co- and countertransport and are critical for establishing the membrane potential. It has been an enigma how Na,K-ATPase discriminates between Na⁺ and K⁺, despite the pumped ion on each side being at a lower concentration than the other ion. Recent crystal structures of analogs of the intermediate conformations E2·Pi·2K⁺ and Na⁺-bound E1∼P·ADP suggest that the dimensions of the respective binding sites in Na,K-ATPase are crucial in determining its selectivity. Here, we found that the selectivity at each membrane face is pH-dependent and

SUBMITTER: Cornelius F 

PROVIDER: S-EPMC5808778 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature