PIP₂-mediated oligomerization of the endosomal sodium/proton exchanger NHE9.

ABSTRACT: The strict exchange of Na⁺ for H⁺ ions across cell membranes is a reaction carried out in almost every cell. Na⁺/H⁺ exchangers that perform this task are physiological homodimers, and whilst the ion transporting domain is highly conserved, their dimerization differs. The Na⁺/H⁺ exchanger NhaA from Escherichia coli has a weak dimerization interface mediated by a β-hairpin domain and with dimer retention dependent on cardiolipin. Similarly, organellar Na⁺/H⁺ exchangers NHE6, NHE7 and NHE9 also contain β-hairpin domains and recent analysis of Equus caballus NHE9 indicated PIP₂ lipids could bind at the dimer interface. However, structural validation of the predicted lipid-mediated oligomerization

SUBMITTER: Kokane S 

PROVIDER: S-EPMC11953442 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature