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EPS8 and E3B1 transduce signals from Ras to Rac

Author

Listed:
  • 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
    Istituto di Microbiologia, University of Bari)

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.

Suggested Citation

  • Giorgio Scita & Johan Nordstrom & Roberta Carbone & Pierluigi Tenca & Giuseppina Giardina & Silvio Gutkind & Mattias Bjarnegård & Christer Betsholtz & Pier Paolo Di Fiore, 1999. "EPS8 and E3B1 transduce signals from Ras to Rac," Nature, Nature, vol. 401(6750), pages 290-293, September.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6750:d:10.1038_45822
    DOI: 10.1038/45822
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