New ChemBioHub paper in Nature Communications: high-resolution structures of NHE6 and NHE9

New in Nature Communications: high-resolution cryo-EM structures of the human endosomal sodium–proton exchangers NHE6 and NHE9.

We resolved human NHE9 and two splice variants of NHE6, mapped the sodium-binding site and uncovered a previously uncharacterised phosphoinositide-binding site in NHE6. The structures provide new insight into how these important regulators of endosomal pH transport ions and interact with their surrounding membrane lipids.

This is a special milestone for us - the first cryo-EM structures from the Huber Lab.

Huge congratulations to co-first authors Jesper Hansen and Ashley Pike, and many thanks to Gamma Chi and David Sauer for helping us enter this exciting new area.

The study brought together an outstanding team across Oxford, CeMM, Johns Hopkins, Geisinger and Bayer, and continues our decade-long collaboration with Bayer. It was enabled by the complementary expertise and resources of the EU-funded ReSOLUTE and EUbOPEN consortia.

📖 Read the paper: https://doi.org/10.1038/s41467-026-77254-0

Cryo-EM structure of human NHE6 showing the transporter, its crown domain and bound lipids. Image © Dr Ashley Pike.