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TitleStructure and elevator mechanism of the mammalian sodium/proton exchanger NHE9.
Journal, issue, pagesEMBO J, Vol. 39, Issue 24, Page e105908, Year 2020
Publish dateDec 15, 2020
AuthorsIven Winklemann / Rei Matsuoka / Pascal F Meier / Denis Shutin / Chenou Zhang / Laura Orellana / Ricky Sexton / Michael Landreh / Carol V Robinson / Oliver Beckstein / David Drew /
PubMed AbstractNa /H exchangers (NHEs) are ancient membrane-bound nanomachines that work to regulate intracellular pH, sodium levels and cell volume. NHE activities contribute to the control of the cell cycle, cell ...Na /H exchangers (NHEs) are ancient membrane-bound nanomachines that work to regulate intracellular pH, sodium levels and cell volume. NHE activities contribute to the control of the cell cycle, cell proliferation, cell migration and vesicle trafficking. NHE dysfunction has been linked to many diseases, and they are targets of pharmaceutical drugs. Despite their fundamental importance to cell homeostasis and human physiology, structural information for the mammalian NHE was lacking. Here, we report the cryogenic electron microscopy structure of NHE isoform 9 (SLC9A9) from Equus caballus at 3.2 Å resolution, an endosomal isoform highly expressed in the brain and associated with autism spectrum (ASD) and attention deficit hyperactivity (ADHD) disorders. Despite low sequence identity, the NHE9 architecture and ion-binding site are remarkably similar to distantly related bacterial Na /H  antiporters with 13 transmembrane segments. Collectively, we reveal the conserved architecture of the NHE ion-binding site, their elevator-like structural transitions, the functional implications of autism disease mutations and the role of phosphoinositide lipids to promote homodimerization that, together, have important physiological ramifications.
External linksEMBO J / PubMed:33118634 / PubMed Central
MethodsEM (single particle)
Resolution3.19 - 3.51 Å
Structure data

11066

6z3y

EMDB-11066, PDB-6z3y:
CryoEM structure of horse sodium/proton exchanger NHE9 in an inward-facing conformation
Method: EM (single particle) / Resolution: 3.51 Å

11067

6z3z

EMDB-11067, PDB-6z3z:
CryoEM structure of horse sodium/proton exchanger NHE9 without C-terminal regulatory domain in an inward-facing conformation
Method: EM (single particle) / Resolution: 3.19 Å

Source
  • equus caballus (horse)
KeywordsMEMBRANE PROTEIN / TRANSPORT PROTEIN

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