In vivo functional analysis of the Ras exchange factor son of sevenless
Biochemistry & Molecular Pharmacology
Graduate School of Biomedical Sciences; Department of Biology and Molecular Biology; Program in Molecular Medicine
Life Sciences | Medicine and Health Sciences
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.
DOI of Published Version
Science. 1995 Apr 28;268(5210):576-9.
Science (New York, N.Y.)
Karlovich CA, Bonfini L, McCollam L, Rogge RD, Daga A, Czech MP, Banerjee U. (1995). In vivo functional analysis of the Ras exchange factor son of sevenless. GSBS Student Publications. https://doi.org/10.1126/science.7725106. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/592