The Grb2 binding domain of mSos1 is not required for downstream signal transduction
| Autor: | Sean E. Egan, Elizabeth M. C. Fisher, Julian Downward, Emilio Porfiri, Wei Wang, James M. Dunn, Qi Jia |
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| Rok vydání: | 1995 |
| Předmět: |
Molecular Sequence Data
genetic processes Son of Sevenless medicine.disease_cause Models Biological Polymerase Chain Reaction Cell Line Transformation Genetic Genetics medicine Animals Guanine Nucleotide Exchange Factors Amino Acid Sequence Frameshift Mutation Alleles Adaptor Proteins Signal Transducing GRB2 Adaptor Protein Mutation Binding Sites Base Sequence biology C-terminus Wild type Proteins DNA biochemical phenomena metabolism and nutrition Rats Cell biology enzymes and coenzymes (carbohydrates) biology.protein bacteria ras Guanine Nucleotide Exchange Factors GRB2 biological phenomena cell phenomena and immunity Signal transduction Function (biology) Protein Binding Signal Transduction Binding domain |
| Zdroj: | Nature Genetics. 10:294-300 |
| ISSN: | 1546-1718 1061-4036 |
| Popis: | Cellular Ras proteins are activated primarily by specific guanine-nucleotide releasing factors such as the Son of Sevenless (Sos) proteins. This activation event is thought to occur in response to plasma membrane localization of a complex containing Sos and a small adapter protein Grb2. We have isolated a dominant mutant allele of mSos1 which transforms Rat1 cells, yet is no longer able to bind Grb2. Biochemical experiments reveal that the subcellular distribution of this truncated Sos protein is not altered with respect to the wild type Sos protein. These data argue against a role for Grb2 in the direct recruitment of Sos proteins to the plasma membrane and suggest that Grb2 may function to overcome negative regulation of Sos by its C terminus. |
| Databáze: | OpenAIRE |
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