{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Seflova J"],"funding":["NHLBI NIH HHS","NIH HHS","NIGMS NIH HHS"],"pagination":["13210-13224"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12433444"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(10)"],"pubmed_abstract":["The sodium-potassium ATPase (Na<sup>+</sup>/K<sup>+</sup>-ATPase, NKA) is a P-type ATPase that plays a central role in cell physiology, establishing Na<sup>+</sup> and K<sup>+</sup> 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)<sub>2</sub>. A structural model of the (alpha beta-PLM)<sub>2</sub> dimer complex suggested key interacting surfaces between the highly conserved alpha subunit M3 helix and the N-terminus of the beta sub"],"journal":["Molecular neurobiology"],"pubmed_title":["The Quaternary Structure of the Sodium Pump Regulatory Complex Is Altered by Mutations of a Site Associated with Familial Hemiplegic Migraine."],"pmcid":["PMC12433444"],"funding_grant_id":["R01HL176212","R01 HL176212","R01 HL158649","R01HL158649","R01GM120142","R01 GM120142"],"pubmed_authors":["Fang X","Espinoza-Fonseca LM","Bossuyt J","Seflova J","Kekenes-Huskey PM","Robia SL"],"additional_accession":[]},"is_claimable":false,"name":"The Quaternary Structure of the Sodium Pump Regulatory Complex Is Altered by Mutations of a Site Associated with Familial Hemiplegic Migraine.","description":"The sodium-potassium ATPase (Na<sup>+</sup>/K<sup>+</sup>-ATPase, NKA) is a P-type ATPase that plays a central role in cell physiology, establishing Na<sup>+</sup> and K<sup>+</sup> 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)<sub>2</sub>. A structural model of the (alpha beta-PLM)<sub>2</sub> dimer complex suggested key interacting surfaces between the highly conserved alpha subunit M3 helix and the N-terminus of the beta sub","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-01T15:45:42.404Z","creation":"2026-04-08T13:47:20.588Z"},"accession":"S-EPMC12433444","cross_references":{"pubmed":["40493343"],"doi":["10.1007/s12035-025-05123-w"]}}