EPS8 and E3B1 transduce signals from Ras to Rac

Giorgio Scita, Johan Nordstrom, Roberta Carbone, Pierluigi Tenca, Giuseppina Giardina, Silvio Gutkind, Mattias Bjarnegård, Christer Betsholtz and Pier Paolo Di Fiore ()
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Giorgio Scita: European Institute of Oncology
Johan Nordstrom: University of Goteborg
Roberta Carbone: European Institute of Oncology
Pierluigi Tenca: European Institute of Oncology
Giuseppina Giardina: European Institute of Oncology
Silvio Gutkind: Molecular Signaling Unit, Laboratory of Cellular Development and Oncology, National Institute of Health
Mattias Bjarnegård: University of Goteborg
Christer Betsholtz: University of Goteborg
Pier Paolo Di Fiore: European Institute of Oncology

Nature, 1999, vol. 401, issue 6750, 290-293

Abstract: Abstract The small guanine nucleotide (GTP)-binding protein Rac regulates mitogen-induced cytoskeletal changes and c-Jun amino-terminal kinase (JNK), and its activity is required for Ras-mediated cell transformation1. Epistatic analysis placed Rac as a key downstream target in Ras signalling2; however, the biochemical mechanism regulating the cross-talk among these small GTP-binding proteins remains to be elucidated. Eps8 (relative molecular mass 97,000) is a substrate of receptors with tyrosine kinase activity3 which binds, through its SH3 domain, to a protein designated E3b1/Abi-1 (refs 4, 5). Here we show that Eps8 and E3b1/Abi-1 participate in the transduction of signals from Ras to Rac, by regulating Rac-specific guanine nucleotide exchange factor (GEF) activities. We also show that Eps8, E3b1 and Sos-1 form a tri-complex in vivo that exhibits Rac-specific GEF activity in vitro. We propose a model in which Eps8 mediates the transfer of signals between Ras and Rac, by forming a complex with E3b1 and Sos-1.

Date: 1999
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DOI: 10.1038/45822

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