Mutational removal of the major site of serine phosphorylation of the epidermal growth factor receptor causes potentiation of signal transduction: role of receptor down-regulation
dc.contributor.author | Theroux, Steven J. | |
dc.contributor.author | Stanley, Krista | |
dc.contributor.author | Campbell, Debra A. | |
dc.contributor.author | Davis, Roger J. | |
dc.date | 2022-08-11T08:09:33.000 | |
dc.date.accessioned | 2022-08-23T16:35:39Z | |
dc.date.available | 2022-08-23T16:35:39Z | |
dc.date.issued | 1992-11-01 | |
dc.date.submitted | 2009-03-24 | |
dc.identifier.citation | <p>Mol Endocrinol. 1992 Nov;6(11):1849-57.</p> | |
dc.identifier.issn | 0888-8809 (Print) | |
dc.identifier.doi | 10.1210/mend.6.11.1480174 | |
dc.identifier.pmid | 1480174 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/38607 | |
dc.description.abstract | The major site of epidermal growth factor receptor (EGF-R) serine phosphorylation is located within the COOH-terminal domain of the receptor at Ser1046/7. We have previously demonstrated that this phosphorylation site accounts for the acute desensitization of the EGF-R observed in EGF-treated cells. Here we show that the mutational removal of this negative regulatory phosphorylation site causes potentiation of signal transduction by the EGF-R. This potentiation can be accounted for in part by a block in the EGF-stimulated down-regulation of the EGF-R. These data indicate that the SER1046/7 phosphorylation site may have a regulatory role during long term incubation of cells with mitogenic concentrations of EGF. | |
dc.language.iso | en_US | |
dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=1480174&dopt=Abstract">Link to Article in PubMed</a></p> | |
dc.relation.url | https://doi.org/10.1210/mend.6.11.1480174 | |
dc.subject | Allosteric Regulation | |
dc.subject | Animals | |
dc.subject | CHO Cells | |
dc.subject | Cell Division | |
dc.subject | Cricetinae | |
dc.subject | Down-Regulation | |
dc.subject | Mutagenesis | |
dc.subject | Phosphorylation | |
dc.subject | *Phosphoserine | |
dc.subject | *Protein Processing, Post-Translational | |
dc.subject | *Signal Transduction | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Mutational removal of the major site of serine phosphorylation of the epidermal growth factor receptor causes potentiation of signal transduction: role of receptor down-regulation | |
dc.type | Journal Article | |
dc.source.journaltitle | Molecular endocrinology (Baltimore, Md.) | |
dc.source.volume | 6 | |
dc.source.issue | 11 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/oapubs/1470 | |
dc.identifier.contextkey | 794967 | |
html.description.abstract | <p>The major site of epidermal growth factor receptor (EGF-R) serine phosphorylation is located within the COOH-terminal domain of the receptor at Ser1046/7. We have previously demonstrated that this phosphorylation site accounts for the acute desensitization of the EGF-R observed in EGF-treated cells. Here we show that the mutational removal of this negative regulatory phosphorylation site causes potentiation of signal transduction by the EGF-R. This potentiation can be accounted for in part by a block in the EGF-stimulated down-regulation of the EGF-R. These data indicate that the SER1046/7 phosphorylation site may have a regulatory role during long term incubation of cells with mitogenic concentrations of EGF.</p> | |
dc.identifier.submissionpath | oapubs/1470 | |
dc.contributor.department | Howard Hughes Medical Institute, Program in Molecular Medicine | |
dc.source.pages | 1849-57 |