Grb7 is a member of a family of molecular adapters which are able to contri
bute positively but also negatively to signal transduction and whose precis
e roles remain obscure. Rnd1 is a member of the Rho family, but, as opposed
to usual GTPases, it is constitutively bound to GTP, We show here that Rnd
1 and Grb7 interact, in two-hybrid assays, in vitro, and in pull-down exper
iments performed with SK-BR3, a breast cancer cell line that overexpresses
Grb7, This interaction involves switch II loop of Rnd1, a region crucial fo
r guanine nucleotide exchange in all GTPases, and a Grb7 SH2 domain, a regi
on crucial for Grb7 interaction with several activated receptors, The contr
ibution of the interaction between Rnd1 and Grb7 to their respective functi
ons and properties is discussed. (C) 2000 Federation of European Biochemica
l Societies.