Display Settings:

Format

Send to:

Choose Destination
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
    J Biol Chem. 1994 Dec 2;269(48):30073-6.

    Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic.

    Source

    Unité 332, INSERM, Paris, France.

    Abstract

    Nef is a 27-kDa myristylated protein conserved in most human immunodeficiency virus (HIV)-1, HIV-2, and simian immunodeficiency virus isolates. Simian immunodeficiency virus Nef is required in macaques for both high viral load and full pathological effects. Nef down-regulates the cell surface expression of CD4 by a post-translational mechanism that is not yet fully elucidated. We have used the yeast two-hybrid system to identify cellular proteins that interact with Nef. A cDNA was isolated which encodes a COOH-terminal fragment of human beta-COP, a major coat component of non-clathrin-coated vesicles. Nef and beta-COP interacted in vitro and were found to be physically associated in HIV-1-infected cells by co-immunoprecipitation. These observations suggest that beta-COP might be one of the cellular mediators of Nef function in HIV-1-infected cells.

    PMID:
    7982906
    [PubMed - indexed for MEDLINE]
    Free full text

      Supplemental Content

      Icon for HighWire

      Save items

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk