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dc.contributor.authorKarlovich, Chris A.
dc.contributor.authorBonfini, Laura
dc.contributor.authorMcCollam, Linda
dc.contributor.authorRogge, Ronald D.
dc.contributor.authorDaga, Andrea
dc.contributor.authorCzech, Michael P.
dc.contributor.authorBanerjee, Utpal
dc.date2022-08-11T08:08:59.000
dc.date.accessioned2022-08-23T16:14:46Z
dc.date.available2022-08-23T16:14:46Z
dc.date.issued1995-04-28
dc.date.submitted2008-10-09
dc.identifier.citation<p>Science. 1995 Apr 28;268(5210):576-9.</p>
dc.identifier.issn0036-8075 (Print)
dc.identifier.doi10.1126/science.7725106
dc.identifier.pmid7725106
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33940
dc.description.abstractThe Son of sevenless (Sos) protein functions as a guanine nucleotide transfer factor for Ras and interacts with the receptor tyrosine kinase Sevenless through the protein Drk, a homolog of mammalian Grb2. In vivo structure-function analysis revealed that the amino terminus of Sos was essential for its function in flies. A molecule lacking the amino terminus was a potent dominant negative. In contrast, a Sos fragment lacking the Drk binding sites was functional and its activity was dependent on the presence of the Sevenless receptor. Furthermore, membrane localization of Sos was independent of Drk. A possible role for Drk as an activator of Sos is discussed and a Drk-independent interaction between Sos and Sevenless is proposed that is likely mediated by the pleckstrin homology domain within the amino terminus.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7725106&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1126/science.7725106
dc.subjectAnimals; Binding Sites; Cell Membrane; Drosophila; *Drosophila Proteins; Eye Proteins; Guanine Nucleotide Exchange Factors; Insect Hormones; Membrane Glycoproteins; Membrane Proteins; Photoreceptors, Invertebrate; Proteins; Receptor Protein-Tyrosine Kinases; Signal Transduction; Son of Sevenless Proteins; ras Guanine Nucleotide Exchange Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleIn vivo functional analysis of the Ras exchange factor son of sevenless
dc.typeJournal Article
dc.source.journaltitleScience (New York, N.Y.)
dc.source.volume268
dc.source.issue5210
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/592
dc.identifier.contextkey646777
html.description.abstract<p>The Son of sevenless (Sos) protein functions as a guanine nucleotide transfer factor for Ras and interacts with the receptor tyrosine kinase Sevenless through the protein Drk, a homolog of mammalian Grb2. In vivo structure-function analysis revealed that the amino terminus of Sos was essential for its function in flies. A molecule lacking the amino terminus was a potent dominant negative. In contrast, a Sos fragment lacking the Drk binding sites was functional and its activity was dependent on the presence of the Sevenless receptor. Furthermore, membrane localization of Sos was independent of Drk. A possible role for Drk as an activator of Sos is discussed and a Drk-independent interaction between Sos and Sevenless is proposed that is likely mediated by the pleckstrin homology domain within the amino terminus.</p>
dc.identifier.submissionpathgsbs_sp/592
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Biology and Molecular Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages576-9


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