# Glutamine binding and sodium coordination reveal the transport mechanism of y⁺LAT1/CD98hc

Source: [nature.com](https://www.nature.com/articles/s41467-026-79388-7) · 2026-11-14 · Life
Page: https://themorning.science/story/glutamine-binding-and-sodium-coordination-reveal-the-transport-mechanism-of-y-la-b8ceaf79d380a4c3
Kind: research · Impact: medium

## In brief

- Cryo-EM, functional and computational studies examine the y⁺LAT1/CD98hc transporter.
- The study describes how the transporter couples sodium binding with substrate recognition, including glutamine.
- The transporter is linked to lysinuric protein intolerance.

## Why it matters

The structural details of how this amino acid transporter selects its substrates and uses sodium could inform future work on transporter function and related disease mechanisms.

## Timeline

- 2026-11-14: Published online in Nature Communications (doi:10.1038/s41467-026-79388-7)

## Coverage

- [Glutamine binding and sodium coordination reveal the transport mechanism of y⁺LAT1/CD98hc](https://www.nature.com/articles/s41467-026-79388-7) — nature.com, 2026-11-14

Tags: cryo-em, amino acid transport, lysinuric protein intolerance, membrane transporters, structural biology

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Brief generated by AI (claude-haiku-5-5) from the reporting listed under Coverage. Headlines belong to their publishers. The Morning Science – https://themorning.science
