Allosteric links between the hydrophilic N-terminus and transmembrane core of human Na⁺ /H⁺ antiporter NHA2.

ABSTRACT: The human Na⁺ /H⁺ antiporter NHA2 (SLC9B2) transports Na⁺ or Li⁺ across the plasma membrane in exchange for protons, and is implicated in various pathologies. It is a 537 amino acids protein with an 82 residues long hydrophilic cytoplasmic N-terminus followed by a transmembrane part comprising 14 transmembrane helices. We optimized the functional expression of HsNHA2 in the plasma membrane of a salt-sensitive Saccharomyces cerevisiae strain and characterized in vivo a set of mutated or truncated versions of HsNHA2 in terms of their substrate specificity, transport activity, localization, and protein stability. We identified a highly conserved proline 246, located in the core of the protein, as being crucial for ion selectivity. The replacement of

SUBMITTER: Velazquez D 

PROVIDER: S-EPMC9667825 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature