Science. 1995 Apr 28;268(5210):576-9.

In vivo functional analysis of the Ras exchange factor son of sevenless.

Karlovich CA, Bonfini L, McCollam L, Rogge RD, Daga A, Czech MP, Banerjee U.

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Department of Biology and Molecular Biology Institute, University of California, Los Angeles 90024, USA.

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.

PMID:: 7725106; [PubMed - indexed for MEDLINE]

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