Show simple item record

dc.contributor.authorGuilherme, Adilson L.
dc.contributor.authorKlarlund, Jes K.
dc.contributor.authorKrystal, Gerald
dc.contributor.authorCzech, Michael P.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:11Z
dc.date.available2022-08-23T16:54:11Z
dc.date.issued1996-11-22
dc.date.submitted2008-08-15
dc.identifier.citation<p>J Biol Chem. 1996 Nov 22;271(47):29533-6.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.271.47.29533
dc.identifier.pmid8939879
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42444
dc.description.abstractPolyphosphoinositides are thought to be mediators of cellular signaling pathways as well as regulators of cytoskeletal elements and membrane trafficking events. It has recently been demonstrated that a class of phosphatidylinositol (PI) 3,4,5-P3 5'-phosphatases contains SH2 domains and proline-rich regions, which are present in many signaling proteins. We report here that insulin stimulation of Chinese hamster ovary cells (CHO-T) expressing human insulin receptors causes an 8-10-fold increase in PI 3,4,5-P3 5'-phosphatase activity in anti-phosphotyrosine immunoprecipitates of the cell lysates. This insulin-sensitive polyphosphoinositide 5'-phosphatase did not catalyze dephosphorylation of PI 4,5-P2. No change in 5'-phosphatase activity was detected in insulin receptor or IRS-1 immune complexes in response to insulin. However, insulin treatment of CHO-T cells markedly increased the PI 3,4,5-P3 5'-phosphatase activity associated with Shc and Grb2. The insulin-regulated polyphosphoinositide 5'-phosphatase was not immunoreactive with antibody raised against the recently cloned SHIP 5'-phosphatase reported to associate with Shc and Grb2 in B lymphocytes. These data demonstrate that insulin causes formation of complexes containing a PI 3,4,5-P3 5'-phosphatase, and Shc or Grb2, or both, suggesting an important role of this enzyme in insulin signaling.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8939879&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.271.47.29533
dc.subjectAnimals
dc.subjectCHO Cells
dc.subjectCricetinae
dc.subjectHumans
dc.subjectInsulin
dc.subjectPhosphoric Monoester Hydrolases
dc.subjectPhosphorylation
dc.subjectPrecipitin Tests
dc.subjectReceptor, Insulin
dc.subjectRecombinant Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRegulation of phosphatidylinositol 3,4,5-trisphosphate 5'-phosphatase activity by insulin
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume271
dc.source.issue47
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/793
dc.identifier.contextkey579673
html.description.abstract<p>Polyphosphoinositides are thought to be mediators of cellular signaling pathways as well as regulators of cytoskeletal elements and membrane trafficking events. It has recently been demonstrated that a class of phosphatidylinositol (PI) 3,4,5-P3 5'-phosphatases contains SH2 domains and proline-rich regions, which are present in many signaling proteins. We report here that insulin stimulation of Chinese hamster ovary cells (CHO-T) expressing human insulin receptors causes an 8-10-fold increase in PI 3,4,5-P3 5'-phosphatase activity in anti-phosphotyrosine immunoprecipitates of the cell lysates. This insulin-sensitive polyphosphoinositide 5'-phosphatase did not catalyze dephosphorylation of PI 4,5-P2. No change in 5'-phosphatase activity was detected in insulin receptor or IRS-1 immune complexes in response to insulin. However, insulin treatment of CHO-T cells markedly increased the PI 3,4,5-P3 5'-phosphatase activity associated with Shc and Grb2. The insulin-regulated polyphosphoinositide 5'-phosphatase was not immunoreactive with antibody raised against the recently cloned SHIP 5'-phosphatase reported to associate with Shc and Grb2 in B lymphocytes. These data demonstrate that insulin causes formation of complexes containing a PI 3,4,5-P3 5'-phosphatase, and Shc or Grb2, or both, suggesting an important role of this enzyme in insulin signaling.</p>
dc.identifier.submissionpathoapubs/793
dc.contributor.departmentProgram in Molecular Medicine and Department of Biochemistry and Molecular Biology
dc.source.pages29533-6


This item appears in the following Collection(s)

Show simple item record