Architecture and autoinhibitory mechanism of the plasma membrane Na⁺/H⁺ antiporter SOS1 in Arabidopsis.

ABSTRACT: Salt-overly-sensitive 1 (SOS1) is a unique electroneutral Na⁺/H⁺ antiporter at the plasma membrane of higher plants and plays a central role in resisting salt stress. SOS1 is kept in a resting state with basal activity and activated upon phosphorylation. Here, we report the structures of SOS1. SOS1 forms a homodimer, with each monomer composed of transmembrane and intracellular domains. We find that SOS1 is locked in an occluded state by shifting of the lateral-gate TM5b toward the dimerization domain, thus shielding the Na⁺/H⁺ binding site. We speculate that the dimerization of the intracellular domain is crucial to stabilize the transporter in this specific conformation. Moreover, two discrete fragments and a residue W1013 are important to prev

SUBMITTER: Wang Y 

PROVIDER: S-EPMC10372031 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature