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

Karlovich, Chris A.
Bonfini, Laura
McCollam, Linda
Rogge, Ronald D.
Daga, Andrea
Czech, Michael P.
Banerjee, Utpal
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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.

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

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10.1126/science.7725106
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7725106
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