Loss of Raf-1-binding activity of v-Ha-Ras by the deletion of amino acid residues 64–72 and 143–151

In order to elucidate the molecular events in signal transduction, examination of the interaction between Ras and Raf-1 seems crucial. Many Raf-1 mutants have been investigated in terms of their binding activities to Ras, where only a few Ras mutants have been examined thus far. We have investigated...

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Bibliographic Details
Published inCellular signalling Vol. 8; no. 5; pp. 393 - 396
Main Authors Hiwasa, Takaki, Kasama, Makoto, Nakadai, Tomoyoshi, Sawada, Toshie, Sakiyama, Shigeru
Format Journal Article
LanguageEnglish
Published England Elsevier Inc 01.08.1996
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Summary:In order to elucidate the molecular events in signal transduction, examination of the interaction between Ras and Raf-1 seems crucial. Many Raf-1 mutants have been investigated in terms of their binding activities to Ras, where only a few Ras mutants have been examined thus far. We have investigated the Raf-1-binding activities of v-Ha-Ras and 21 insertion/deletion mutants of this protein. The results show that the mutants have varying levels of Raf-1-binding activity that are related neither to their transforming activity nor to their guanine nucleotide-binding activity. Deletion in the effector domain of Ras did not completely abolish Raf-1-binding, whereas the deletion in amino acid residues 64–72 or 143–151 resulted in complete loss of Raf-1-binding activity.
ISSN:0898-6568
1873-3913
DOI:10.1016/0898-6568(96)00078-2