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J. Biol. Chem., Vol. 267, Issue 17, 11677-11680, 06, 1992
P Lang, L Guizani, I Vitte-Mony, R Stancou, O Dorseuil, G Gacon and J Bertoglio
The Rho proteins are identified as a subgroup of the Ras superfamily of low
molecular weight GTP-binding proteins. We have studied the expression of
these proteins in human cytotoxic natural killer cells and found that RhoA
is the most abundantly expressed member of the Rho family. The Rho proteins
are specific substrates for ADP-ribosylation catalyzed by the C3 exoenzyme
from Clostridium botulinum. We report here that introduction of recombinant
C3 in electropermeabilized natural killer cells or in cytotoxic T
lymphocytes resulted in a dose- dependent inhibition of their cytolytic
function. Furthermore, a single substrate is efficiently ADP-ribosylated by
C3 in extracts from cytotoxic cells. Biochemical analyses indicate that
this substrate is RhoA, and subcellular fractionation experiments
demonstrate that it is essentially present in the cytosol of the cells.
Western blot analysis, however, revealed that a small proportion of the Rho
protein can be found associated with the cell membrane as well as with the
cytotoxic granules. These results indicate that the low molecular weight
GTP- binding protein RhoA is present in cytotoxic lymphocytes and plays a
critical role in cell-mediated cytotoxicity.
ADP-ribosylation of the ras-related, GTP-binding protein RhoA inhibits lymphocyte-mediated cytotoxicity
Institut National de la Sante et de la Recherche Medicale (INSERM), Unite 333, Institut Gustave Roussy, Villejuif, France.
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