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Transport of cationic amino acids by the mouse ecotropic retrovirus receptor

Naturevolume 352pages725728 (1991) | Download Citation

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Abstract

SUSCEPTIBILITY of rodent cells to infection by ecotropic murine leukaemia viruses (MuLV) is determined by binding of the virus envelope to a membrane receptor that has multiple membrane-spanning domains1. Cells infected by ecotropic MuLV synthesize envelope protein, gp70, which binds to this receptor, thereby preventing additional infections. The consequences of envelope-MuLV receptor binding for the infected host cell have not been directly determined, partly because the cellular function of the MuLV receptor protein is unknown. Here we report a coincidence in the positions of the first eight putative membrane-spanning domains found in the virus receptor1 and in two related proteins2, the arginine2–4 and histidine2,3,5 permeases of Saccharomyces cerevisiae (Fig. 1), but not in any other proteins identified by computer-based sequence comparison of the Gen Bank data base1. Xenopus oocytes injected with receptor-encoding messenger RNA show increased uptake of L-arginine, L-lysine and L-ornithine. The transport properties and the expression pattern of the virus receptor behave in ways previously attributed to y+ (refs 6, 7), the principal transporter of cationic L-amino acids in mammalian cells.

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  1. Howard Hughes Medical Institute and Division of Hematology, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, 75 Francis Street, Boston, Massachusetts, 02115, USA

    • Jung Woo Kim
    • , Ellen I. Closs
    • , Lorraine M. Albritton
    •  & James M. Cunningham

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https://doi.org/10.1038/352725a0

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