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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/1652061 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1652061 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1652061 | http://www.w3.org/2000/01/rdf-schema#comment | "The receptor for colony-stimulating factor-1 (CSF-1) is a receptor protein-tyrosine kinase. To study the possible function of CSF-1 receptor autophosphorylation, two autophosphorylation sites, Tyr-706, located in the kinase insert, and Tyr-807, a residue conserved in all protein-tyrosine kinases, were changed independently to either phenylalanine or glycine. Wild-type and mutant receptors were stably expressed in Rat-2 cells. In response to CSF-1, cells expressing Phe- or Gly-706 mutant receptors showed increased growth rate and altered cell morphology. Both the Phe- and Gly-706 mutant receptors associated with and phosphorylated phosphatidylinositol-3 kinase at levels comparable with those of wild-type receptors. However, these mutant receptors differed subtly from each other and from the wild-type receptor in their ability to induce different aspects of the response to CSF-1. The Phe-706 mutant receptor was most strongly affected in its ability to increase growth rate or elevate the levels of c-fos and NGF1A mRNAs, whereas the Gly-706 mutant receptor was most markedly affected in its ability to induce a change in cell morphology or increase the levels of c-jun and NGF1A mRNAs. These findings indicate that Tyr-706 itself, or this region of the receptor, may be important for interaction of the CSF-1 receptor with different signalling pathways. Gly-807 mutant receptors lacked protein-tyrosine kinase activity, failed to respond to CSF-1, and were defective in biosynthetic processing. Phe-807 mutant receptors had 40 to 60% reduced protein-tyrosine kinase activity in vitro. Although cells expressing Phe-807 receptors were able to respond to CSF-1, the changes in growth rate and cell morphology were significantly less than seen with wild-type receptors, and the induction of early response genes was also slightly lower than for the wild-type receptor. In contrast, Phe-807 receptors were equivalent to wild-type receptors when tested for their ability to interact with phosphatidylinositol-3 kinase. These findings indicate that phosphorylation of Tyr-807 may be important for full activation of the receptor."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.11.9.4698-4709.1991"xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.11.9.4698-4709.1991"xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/author | "Hunter T."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/author | "Hunter T."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/author | "van der Geer P."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/author | "van der Geer P."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/date | "1991"xsd:gYear |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/date | "1991"xsd:gYear |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/pages | "4698-4709"xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/pages | "4698-4709"xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/title | "Tyrosine 706 and 807 phosphorylation site mutants in the murine colony-stimulating factor-1 receptor are unaffected in their ability to bind or phosphorylate phosphatidylinositol-3 kinase but show differential defects in their ability to induce early response gene transcription."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/title | "Tyrosine 706 and 807 phosphorylation site mutants in the murine colony-stimulating factor-1 receptor are unaffected in their ability to bind or phosphorylate phosphatidylinositol-3 kinase but show differential defects in their ability to induce early response gene transcription."xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/volume | "11"xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://purl.uniprot.org/core/volume | "11"xsd:string |
| http://purl.uniprot.org/citations/1652061 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1652061 |
| http://purl.uniprot.org/citations/1652061 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1652061 |
| http://purl.uniprot.org/citations/1652061 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1652061 |
| http://purl.uniprot.org/citations/1652061 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1652061 |
| http://purl.uniprot.org/uniprot/P09581 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1652061 |
| http://purl.uniprot.org/uniprot/P09581#attribution-8CA6CE26357AD8C617787AD1F1B56131 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1652061 |