Cryo-EM structure of the human neutral amino acid transporter ASCT2

Garaeva, Alisa A.; Oostergetel, Gert T.; Gati, Cornelius; Guskov, Albert; Paulino, Cristina; Slotboom, Dirk J.

doi:10.1038/s41594-018-0076-y

Title: Cryo-EM structure of the human neutral amino acid transporter ASCT2

Journal Article · 04 June 2018 · Nature Structural & Molecular Biology

DOI: https://doi.org/10.1038/s41594-018-0076-y · OSTI ID:1475494

Garaeva, Alisa A. ^[1];

^[1]; Gati, Cornelius ^[2];

^[1]; Paulino, Cristina ^[1];

^[1]

Univ. of Groningen, Groningen (The Netherlands)
SLAC National Accelerator Lab., Menlo Park, CA (United States); Stanford Univ., Stanford, CA (United States)

Human ASCT2 belongs to the SLC1 family of secondary transporters and is specific for the transport of small neutral amino acids. ASCT2 is upregulated in cancer cells and serves as the receptor for many retroviruses; hence, it has importance as a potential drug target. Here we used single-particle cryo-EM to determine a structure of the functional and unmodified human ASCT2 at 3.85-Å resolution. ASCT2 forms a homotrimeric complex in which each subunit contains a transport and a scaffold domain. Prominent extracellular extensions on the scaffold domain form the predicted docking site for retroviruses. Relative to structures of other SLC1 members, ASCT2 is in the most extreme inward-oriented state, with the transport domain largely detached from the central scaffold domain on the cytoplasmic side. In conclusion, this domain detachment may be required for substrate binding and release on the intracellular side of the membrane.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1475494

Journal Information:: Nature Structural & Molecular Biology, Journal Name: Nature Structural & Molecular Biology Journal Issue: 6 Vol. 25; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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