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

DOI: 10.1038/s41467-018-03066-6 DOI Help

Authors: Katharina E. J. Jungnickel (University of Oxford) , Joanne Parker (University of Oxford) , Simon Newstead (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 9

State: Published (Approved)
Published: February 2018
Diamond Proposal Number(s): 12346 , 18069

Open Access Open Access

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.

Journal Keywords: Biochemistry; X-ray crystallography

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I23-Long wavelength MX , I24-Microfocus Macromolecular Crystallography

Other Facilities: Soleil; Photon Factory

Documents:
s41467-018-03066-6.pdf