In vivo functional analysis of the Ras exchange factor son of sevenless
dc.contributor.author | Karlovich, Chris A. | |
dc.contributor.author | Bonfini, Laura | |
dc.contributor.author | McCollam, Linda | |
dc.contributor.author | Rogge, Ronald D. | |
dc.contributor.author | Daga, Andrea | |
dc.contributor.author | Czech, Michael P. | |
dc.contributor.author | Banerjee, Utpal | |
dc.date | 2022-08-11T08:08:59.000 | |
dc.date.accessioned | 2022-08-23T16:14:46Z | |
dc.date.available | 2022-08-23T16:14:46Z | |
dc.date.issued | 1995-04-28 | |
dc.date.submitted | 2008-10-09 | |
dc.identifier.citation | <p>Science. 1995 Apr 28;268(5210):576-9.</p> | |
dc.identifier.issn | 0036-8075 (Print) | |
dc.identifier.doi | 10.1126/science.7725106 | |
dc.identifier.pmid | 7725106 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/33940 | |
dc.description.abstract | 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. | |
dc.language.iso | en_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.url | https://doi.org/10.1126/science.7725106 | |
dc.subject | Animals; 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.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | In vivo functional analysis of the Ras exchange factor son of sevenless | |
dc.type | Journal Article | |
dc.source.journaltitle | Science (New York, N.Y.) | |
dc.source.volume | 268 | |
dc.source.issue | 5210 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/592 | |
dc.identifier.contextkey | 646777 | |
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.submissionpath | gsbs_sp/592 | |
dc.contributor.department | Program in Molecular Medicine | |
dc.contributor.department | Department of Biology and Molecular Biology | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 576-9 |