Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor. (Articolo in rivista)

Type
Label
  • Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor. (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Alternative label
  • Gallina A, Rossi F, Milanesi G. (2001)
    Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor.
    in Virology (N.Y.N.Y., Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Gallina A, Rossi F, Milanesi G. (literal)
Pagina inizio
  • 7 (literal)
Pagina fine
  • 18 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 283 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor. (literal)
Abstract
  • Nef proteins of primate immunodeficiency viruses exert pleiotropic effects, such as enhanced endocytosis of CD4 and MHC-I cell surface molecules, perturbation of signal transduction cascades, and virion infectivity enhancement. Nef function intersects that of a number of cell kinases, including C kinases (PKCs) and Src-family kinases. Here the interaction of HIV-1 Nef with Rack1 (receptor for activated C kinase 1) is reported. Nef binds the Rack1 C-terminal moiety in a yeast two-hybrid system and in cell-free pull-down assays and copurifies with in vitro translated Rack1. Nef and Rack1 partially colocalize on the trans-Golgi network and plasma membranes. The presence of Rack1 doubles Nef phosphorylation by PKCs in vitro. Our data agree with the idea that Rack1 acts as a Nef intracellular docking site, bringing Nef and PKCs together. Other signal transduction or endocytosis proteins, in particular Src-like kinases, might meet Nef by intermediation of the Rack1 adaptor. Copyright 2001 Academic Press. (literal)
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