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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/9441

Title: A Drosophila SH2-SH3 Adaptor Protein Implicated in Coupling the Sevenless Tyrosine Kinase to an Activator of Ras Guanine Nucleotide Exchange, Sos
Authors: Olivier, Jean Paul
Raabe, Thomas
Henkerneyer, Mark
Dickson, Barry
Mbamalu, Geraldine
Margolis, Ben
Schlessinger, Joseph
Hafen, Ernst
Pawson, Tony
Keywords: Drosophila Proteins
Receptor Protein-Tyrosine Kinases
Signal Transduction
Issue Date: 9-Apr-1993
Publisher: Cell Press
Citation: Cell. 1993 Apr 9;73(1):179-91.
Abstract: A Drosophila gene (drk) encodes a widely expressed protein with a single SH2 domain and two flanking SH3 domains, which is homologous to the Sem-5 protein of C. elegans and mammalian GRB2. Genetic analysis suggests that drk function is essential for signaling by the sevenless receptor tyrosine kinase. Drk biological activity correlates with binding of its SH2 domain to activated receptor tyrosine kinases and concomitant localization of drk to the plasma membrane. In vitro, drk also binds directly to the C-terminal tail of Sos, a Ras guanine nucleotide-releasing protein (GNRP), which, like Rasl and drk, is required for sevenless signaling. These results suggest that drk binds autophosphorylated receptor tyrosine kinases with its SH2 domain and the Sos GNRP through its Ski3 domains, thereby coupling receptor tyrosine kinases to Ras activation. The conservation of these signaling proteins during evolution indicates that this is a general mechanism for linking tyrosine kinases to Ras.
URI: http://www.cell.com/
Appears in Collections:Pawson, Tony
Pawson, Tony

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