In vivo functional analysis of the Ras exchange factor Son of sevenless

C. A. Karlovich, L. Bonfini, L. McCollam, R. D. Rogge, A. Daga, M. P. Czech, U. Banerjee

Research output: Contribution to journalArticlepeer-review

Abstract

The Son of sevenless (Sos) protein functions as a guanine nucleotide transfer factor for Ras and interacts with the receptor tyrosine kinase Sevenless through the protein Drk, a homolog of mammalian Grb2. In vivo structure-function analysis revealed that the amino terminus of Sos was essential for its function in flies. A molecule lacking the amino terminus was a potent dominant negative. In contrast, a Sos fragment lacking the Drk binding sites was functional and its activity was dependent on the presence of the Sevenless receptor. Furthermore, membrane localization of Sos was independent of Drk. A possible role for Drk as an activator of Sos is discussed and a Drk-independent interaction between Sos and Sevenless is proposed that is likely mediated by the pleckstrin homology domain within the amino terminus.

Original languageEnglish
Pages (from-to)576-579
Number of pages4
JournalScience
Volume268
Issue number5210
Publication statusPublished - 1995

ASJC Scopus subject areas

  • General

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