The Quaternary Structure of the Sodium Pump Regulatory Complex Is Altered by Mutations of a Site Associated with Familial Hemiplegic Migraine.

ABSTRACT: The sodium-potassium ATPase (Na⁺/K⁺-ATPase, NKA) is a P-type ATPase that plays a central role in cell physiology, establishing Na⁺ and K⁺ gradients across the plasma membrane. We have previously investigated the assembly of the NKA complex, quantifying interactions of the catalytic subunit, alpha, with its accessory subunit, beta, and a regulatory microprotein from the FXYD family, phospholemman (PLM). We also investigated the dimerization of alpha subunits, together with accessory proteins, in a larger complex with stoichiometry (alpha beta-PLM)₂. A structural model of the (alpha beta-PLM)₂ dimer complex suggested key interacting surfaces between the highly conserved alpha subunit M3 helix and the N-terminus of the beta sub

SUBMITTER: Seflova J 

PROVIDER: S-EPMC12433444 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature