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2022 - Structure, mechanism and lipid-mediated remodeling of the mammalian Na+/H+ exchanger NHA2

 Icon N1   SURFE2R N1 publication in Nature Structural & Molecular Biology (2022)

Authors:
Matsuoka R., Fudim R., Jung S., Zhang C., Bazzone A., Chatzikyriakidou Y., Robinson C. V., Nomura N., Iwata S., Landreh M., Orellana L., Beckstein O., Drew D.

Journal:
Nature Structural & Molecular Biology (2022) doi:10.1016/j.bios.2021.113763


Abstract: 

The Na+/H+ exchanger SLC9B2, also known as NHA2, correlates with the long-sought-after Na+/Li+ exchanger linked to the pathogenesis of diabetes mellitus and essential hypertension in humans. Despite the functional importance of NHA2, structural information and the molecular basis for its ion-exchange mechanism have been lacking. Here we report the cryo-EM structures of bison NHA2 in detergent and in nanodiscs, at 3.0 and 3.5 Å resolution, respectively. The bison NHA2 structure, together with solid-state membrane-based electrophysiology, establishes the molecular basis for electroneutral ion exchange. NHA2 consists of 14 transmembrane (TM) segments, rather than the 13 TMs previously observed in mammalian Na+/H+ exchangers (NHEs) and related bacterial antiporters. The additional N-terminal helix in NHA2 forms a unique homodimer interface with a large intracellular gap between the protomers, which closes in the presence of phosphoinositol lipids. We propose that the additional N-terminal helix has evolved as a lipid-mediated remodeling switch for the regulation of NHA2 activity.


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