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dc.contributor.authorTheroux, Steven J.
dc.contributor.authorStanley, Krista
dc.contributor.authorCampbell, Debra A.
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:09:33.000
dc.date.accessioned2022-08-23T16:35:39Z
dc.date.available2022-08-23T16:35:39Z
dc.date.issued1992-11-01
dc.date.submitted2009-03-24
dc.identifier.citation<p>Mol Endocrinol. 1992 Nov;6(11):1849-57.</p>
dc.identifier.issn0888-8809 (Print)
dc.identifier.doi10.1210/mend.6.11.1480174
dc.identifier.pmid1480174
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38607
dc.description.abstractThe 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.isoen_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.urlhttps://doi.org/10.1210/mend.6.11.1480174
dc.subjectAllosteric Regulation
dc.subjectAnimals
dc.subjectCHO Cells
dc.subjectCell Division
dc.subjectCricetinae
dc.subjectDown-Regulation
dc.subjectMutagenesis
dc.subjectPhosphorylation
dc.subject*Phosphoserine
dc.subject*Protein Processing, Post-Translational
dc.subject*Signal Transduction
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMutational 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.typeJournal Article
dc.source.journaltitleMolecular endocrinology (Baltimore, Md.)
dc.source.volume6
dc.source.issue11
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1470
dc.identifier.contextkey794967
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.submissionpathoapubs/1470
dc.contributor.departmentHoward Hughes Medical Institute, Program in Molecular Medicine
dc.source.pages1849-57


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