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Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family
Author(s) -
Vayssière Béatrice,
Zalcman Gérard,
Mahé Yannick,
Mirey Gladys,
Ligensa Tanja,
Weidner K.Michael,
Chardin Pierre,
Camonis Jacques
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01530-6
Subject(s) - guanine nucleotide exchange factor , gtpase , signal transducing adaptor protein , signal transduction , microbiology and biotechnology , gtpase activating protein , biology , chemistry , g protein
Grb7 is a member of a family of molecular adapters which are able to contribute positively but also negatively to signal transduction and whose precise 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 Rnd1 and Grb7 interact, in two‐hybrid assays, in vitro, and in pull‐down experiments performed with SK‐BR3, a breast cancer cell line that overexpresses Grb7. This interaction involves switch II loop of Rnd1, a region crucial for guanine nucleotide exchange in all GTPases, and a Grb7 SH2 domain, a region crucial for Grb7 interaction with several activated receptors. The contribution of the interaction between Rnd1 and Grb7 to their respective functions and properties is discussed.