Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state

Recent advances in understanding intracellular amino acid transport and mechanistic target of rapamycin complex 1 (mTORC1) signaling shed light on solute carrier 38, family A member 9 (SLC38A9), a lysosomal transporter responsible for the binding and translocation of several essential amino acids. Here we present the first crystal structure of SLC38A9 from Danio rerio in complex with arginine. As captured in the cytosol-open state, the bound arginine was locked in a transitional state stabilized by transmembrane helix 1 (TM1) of drSLC38A9, which was anchored at the groove between TM5 and TM7.

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Lei, H. T., et al. (2018). Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state. Nature structural & molecular biology. https://doi.org/10.1038/s41594-018-0072-2

@article{LEI2018,
  author       = {Lei, H. T. and Gonen, T. and others},
  title        = {{Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state}},
  journal      = {Nature structural & molecular biology},
  year         = {2018},
  doi          = {10.1038/s41594-018-0072-2},
  note         = {PMID: 29872228},
}

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Barton, O. (2026). Oliver's mTOR Atlas (record LEI2018) [Data set]. https://mtor-atlas.org/study/LEI2018/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_LEI2018,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record LEI2018},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/LEI2018/},
  doi          = {10.5281/zenodo.22059963}
}