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http://hdl.handle.net/2445/177648
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DC Field | Value | Language |
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dc.contributor.author | Soler Prat, Concepció | - |
dc.contributor.author | Beguinot, Laura | - |
dc.contributor.author | Sorkin, Alexander | - |
dc.contributor.author | Carpenter, Graham | - |
dc.date.accessioned | 2021-05-26T15:28:00Z | - |
dc.date.available | 2021-05-26T15:28:00Z | - |
dc.date.issued | 1993-10-15 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/2445/177648 | - |
dc.description.abstract | The importance of the carboxyl-terminal domain of the epidermal growth factor (EGF) receptor and its five autophosphorylation sites in the in vivo interaction and tyrosine phosphorylation of the ras GTPase-activating protein (rasGAP) has been investigated, using NIH 3T3 cells transfected with mutant EGF receptors. Phosphorylation of rasGAP by EGF receptor mutants, in which one to four autophosphorylation sites (Tyr-1173, -1148, -1086, and -1068) were mutated to phenylalanine, was reduced by 50-60% compared to the wild-type receptor. Elimination of these four autophosphorylation sites by truncation of 123 carboxyl-terminal residues of the EGF receptor paralleled results obtained with point mutants. Substantial inhibition (about 90%) of rasGAP tyrosine phosphorylation by the EGF receptor occurred only when the remaining autophosphorylation site (Tyr-992) was mutated, in the context of this truncated receptor or in the full-length receptor mutated at all four other autophosphorylation sites. However, a point mutation of only Tyr-992 in the full-length receptor suppressed tyrosine phosphorylation of rasGAP only by 50%. In contrast, an EGF receptor lacking the last 214 amino acid residues (Dc214), which encompasses all five autophosphorylation sites, phosphorylated rasGAP to the same extent as the wild-type receptor. However, this truncated receptor was significantly impaired in its capacity to phosphorylate phospholipase C-gamma 1. Interestingly, while EGF receptor autophosphorylation sites are required for EGF-induced rasGAP association with the receptor, maximal phosphorylation of rasGAP by the truncated receptor Dc214 occurred without detectable formation of receptor-rasGAP complexes. Furthermore, the capacity of mutated EGF receptors to bring about focal transformation was correlated with their capacity to phosphorylate rasGAP. | - |
dc.format.extent | 10 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation.isformatof | Reproducció del document publicat a: https://www.jbc.org/issue/S0021-9258(20)X6719-6 | - |
dc.relation.ispartof | Journal of Biological Chemistry, 1993, vol. 268, num. 29, p. 22010-22019 | - |
dc.rights | (c) American Society for Biochemistry and Molecular Biology, 1993 | - |
dc.source | Articles publicats en revistes (Patologia i Terapèutica Experimental) | - |
dc.subject.classification | Proteïnes | - |
dc.subject.classification | Proteïna-tirosina-fosfatasa | - |
dc.subject.classification | Metabolisme | - |
dc.subject.other | Proteins | - |
dc.subject.other | Protein-tyrosine phosphatase | - |
dc.subject.other | Metabolism | - |
dc.title | Tyrosine phosphorylation of ras GTPase activating protein does not require association with the epidermal growth factor receptor | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 087489 | - |
dc.date.updated | 2021-05-26T15:28:00Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 8408058 | - |
Appears in Collections: | Articles publicats en revistes (Patologia i Terapèutica Experimental) |
Files in This Item:
File | Description | Size | Format | |
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087489.pdf | 6.92 MB | Adobe PDF | View/Open |
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