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GGA and arf proteins modulate retrovirus assembly and release

  1. Author:
    Joshi, A.
    Garg, H.
    Nagashima, K.
    Bonifacino, J. S.
    Freed, E. O.

  2. Author Address

    Joshi, Anjali, Freed, Eric O.] NCI, HIV Drug Resistance Program, Virus Cell Interact Sect, Frederick, MD 21702 USA. [Garg, Himanshu] NCI, Ctr Canc Res, Frederick, MD 21702 USA. [Nagashima, Kunio] NCI, SAIC Frederick, Adv Technol Program, Image Anal Lab, Frederick, MD 21702 USA. [Bonifacino, Juan S.] NICHHD, Cell Biol & Metab Branch, NIH, Bethesda, MD 20892 USA.
    1. Year: 2008
  2. Journal: Molecular Cell
    1. 30
    2. 2
    3. Pages: 227-238
  4. Type of Article: Article
  1. Abstract:

    The Gag protein is the major structural determinant of retrovirus assembly. Although a number of cellular factors have been reported to facilitate retrovirus release, little is known about the cellular machinery that directs Gag to the site of virus assembly. Here, we report roles for the Golgi-localized gamma-ear containing Arf-binding (GGA) and ADP ribosylation factor (Arf) proteins in retrovirus particle assembly and release. Whereas siRNA-mediated depletion of GGA2 and GGA3 led to a significant increase in particle release in a late domain-dependent manner, GGA overexpression severely reduced retrovirus particle production by impairing Gag trafficking to the membrane. GGA overexpression inhibited retroviral assembly and release by disrupting Arf protein activity. Furthermore, disruption of endogenous Arf activity inhibited particle production by decreasing Gag-membrane binding. These findings identify the GGA proteins as modulators of HIV-1 release and the Arf proteins as critical cellular cofactors in retroviral Gag trafficking to the plasma membrane.

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External Sources

  1. PMID: 18439901

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