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Structural basis for amino acid transport by the CAT family of SLC7 transporters

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  • Katharina E. J. Jungnickel

    (University of Oxford)

  • Joanne L. Parker

    (University of Oxford)

  • Simon Newstead

    (University of Oxford)

Abstract

Amino acids play essential roles in cell biology as regulators of metabolic pathways. Arginine in particular is a major signalling molecule inside the cell, being a precursor for both l-ornithine and nitric oxide (NO) synthesis and a key regulator of the mTORC1 pathway. In mammals, cellular arginine availability is determined by members of the solute carrier (SLC) 7 family of cationic amino acid transporters. Whereas CAT-1 functions to supply cationic amino acids for cellular metabolism, CAT-2A and -2B are required for macrophage activation and play important roles in regulating inflammation. Here, we present the crystal structure of a close homologue of the mammalian CAT transporters that reveals how these proteins specifically recognise arginine. Our structural and functional data provide a model for cationic amino acid transport in mammalian cells and reveals mechanistic insights into proton-coupled, sodium-independent amino acid transport in the wider APC superfamily.

Suggested Citation

  • Katharina E. J. Jungnickel & Joanne L. Parker & Simon Newstead, 2018. "Structural basis for amino acid transport by the CAT family of SLC7 transporters," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03066-6
    DOI: 10.1038/s41467-018-03066-6
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    Cited by:

    1. Lior Artzi & Assaf Alon & Kelly P. Brock & Anna G. Green & Amy Tam & Fernando H. Ramírez-Guadiana & Debora Marks & Andrew Kruse & David Z. Rudner, 2021. "Dormant spores sense amino acids through the B subunits of their germination receptors," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    2. Josep Rullo-Tubau & Maria Martinez-Molledo & Paola Bartoccioni & Ignasi Puch-Giner & Ángela Arias & Suwipa Saen-Oon & Camille Stephan-Otto Attolini & Rafael Artuch & Lucía Díaz & Víctor Guallar & Ekai, 2024. "Structure and mechanisms of transport of human Asc1/CD98hc amino acid transporter," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Yongchan Lee & Pattama Wiriyasermkul & Pornparn Kongpracha & Satomi Moriyama & Deryck J. Mills & Werner Kühlbrandt & Shushi Nagamori, 2022. "Ca2+-mediated higher-order assembly of heterodimers in amino acid transport system b0,+ biogenesis and cystinuria," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    4. Joanne L. Parker & Justin C. Deme & Dimitrios Kolokouris & Gabriel Kuteyi & Philip C. Biggin & Susan M. Lea & Simon Newstead, 2021. "Molecular basis for redox control by the human cystine/glutamate antiporter system xc−," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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