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Science 28 April 1995:
Vol. 268. no. 5210, pp. 576 - 579
DOI: 10.1126/science.7725106
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Articles

Science, Vol 268, Issue 5210, 576-579
Copyright © 1995 by American Association for the Advancement of Science

articles

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

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

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

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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Insulin and Epidermal Growth Factor Receptors Regulate Distinct Pools of Grb2-SOS in the Control of Ras Activation.
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Functional Roles for the Pleckstrin and Dbl Homology Regions in the Ras Exchange Factor Son-of-sevenless.
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