Substrate recognition and transport mechanism of the human proton-coupled amino-acid transporter 1 (SLC36A1)

Yin J, Zhang S, Liu C, Xie M, Gao Y, Chen M, Wang Y, Chen M, Fan H, Yang Z, Li H, …, Yang M · 2026 · Nature Communications · Atlas ID YIN2026

What this study shows

Cryo-EM structures of human PAT1 (SLC36A1) in apo and substrate-bound states reveal a convergent binding mode for diverse zwitterionic amino acids. This is a structural study; PAT1's role in lysosomal amino acid export and mTORC1 activation comes from earlier work.

Abstract

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The proton-coupled amino-acid transporter SLC36A1 (hPAT1) is an atypical H+-driven carrier and mediates the intestinal absorption of a wide array of zwitterionic amino-acid analogs, including many compounds with central nervous-system (CNS) activity, as well as the activation of the mTORC1 pathway and the export of amino acids from lysosomes, thereby maintaining cellular amino-acid homeostasis.

Read the full abstract on PubMed →

At a glance

Evidence type	M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Recombinant human protein (cryo-EM)) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is.
Study type	5 - Mechanistic / In Vitro
Model system	Recombinant human protein (cryo-EM)
Journal	Nature Communications
Year	2026
Peer reviewed	Yes
Record last updated	2026-10-01
Source	DOI 10.1038/s41467-026-75306-z · PMID 42414312

Extracted findings

These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.

Intervention	Structural/biochemical (cryo-EM of SLC36A1/PAT1, apo + 3 substrate-bound states)
Target	SLC36A1 (PAT1) / lysosomal amino acid efflux / mTORC1 activation
Model	Human (recombinant protein, cryo-EM; no animal/cell phenotype data)
Effect	Reveals the structural basis for the substrate promiscuity of PAT1; its role in lysosomal amino acid export and mTORC1 activation is prior work

In the Atlas

Cite this paper

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Yin, J., Zhang, S., Liu, C., Xie, M., Gao, Y., Chen, M., Wang, Y., Chen, M., Fan, H., Yang, Z., Li, H., Liang, L., Zhou, B., Chen, X., & Yang, M. (2026). Substrate recognition and transport mechanism of the human proton-coupled amino-acid transporter 1 (SLC36A1). Nature Communications. https://doi.org/10.1038/s41467-026-75306-z

@article{YIN2026,
  author       = {Yin, J. and Zhang, S. and Liu, C. and Xie, M. and Gao, Y. and Chen, M. and Wang, Y. and Chen, M. and Fan, H. and Yang, Z. and Li, H. and Liang, L. and Zhou, B. and Chen, X. and Yang, M.},
  title        = {{Substrate recognition and transport mechanism of the human proton-coupled amino-acid transporter 1 (SLC36A1)}},
  journal      = {Nature Communications},
  year         = {2026},
  doi          = {10.1038/s41467-026-75306-z},
  note         = {PMID: 42414312},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record YIN2026) [Data set]. https://mtor-atlas.org/study/YIN2026/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_YIN2026,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record YIN2026},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/YIN2026/},
  doi          = {10.5281/zenodo.22059963}
}

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