Show simple item record

dc.contributor.authorDavis, Roger J.
dc.contributor.authorMeisner, Herman
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:44Z
dc.date.available2022-08-23T16:54:44Z
dc.date.issued1987-11-25
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1987 Nov 25;262(33):16041-7.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid3119581
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42568
dc.description.abstractTreatment of Swiss 3T3 fibroblasts with tumor-promoting phorbol diester or with platelet-derived growth factor caused the phosphorylation of the transferrin receptor by protein kinase C (Ca2+/phospholipid-dependent enzyme) at serine 24 and increased the cell surface expression of the transferrin receptor. The hypothesis that the regulation of transferrin receptor cycling by protein kinase C is causally related to the phosphorylation of the receptor at serine 24 was critically tested. Site-directed mutagenesis of the human transferrin receptor cDNA was used to substitute serine 24 with threonine or alanine residues in order to create phosphorylation defective receptors. Wild-type and mutated transferrin receptors were expressed in Swiss 3T3 fibroblasts using the retrovirus vector pZipNeoSV (X). These receptors were functionally active and caused the receptor-mediated endocytosis of diferric transferrin. Incubation of the fibroblasts with phorbol diester caused the phosphorylation of the wild-type (Ser-24) human transferrin receptor, but this treatment did not result in the phosphorylation of the mutated (Ala-24 and Thr-24) receptors. The cycling of the phosphorylation defective receptors was regulated by phorbol diester and platelet-derived growth factor in a manner similar to that observed for the wild-type receptor. We conclude that the regulation of transferrin receptor cycling by protein kinase C is independent of receptor phosphorylation at serine 24 in Swiss 3T3 fibroblasts.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3119581&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/262/33/16041.full.pdf+html
dc.subjectAnimals
dc.subjectCells, Cultured
dc.subjectClone Cells
dc.subjectFibroblasts
dc.subjectHomeostasis
dc.subjectHumans
dc.subjectKinetics
dc.subjectMice
dc.subjectMutation
dc.subjectPhosphorylation
dc.subjectPlatelet-Derived Growth Factor
dc.subjectProtein Kinase C
dc.subjectReceptors, Transferrin
dc.subject*Serine
dc.subjectTetradecanoylphorbol Acetate
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRegulation of transferrin receptor cycling by protein kinase C is independent of receptor phosphorylation at serine 24 in Swiss 3T3 fibroblasts
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume262
dc.source.issue33
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/904
dc.identifier.contextkey579793
html.description.abstract<p>Treatment of Swiss 3T3 fibroblasts with tumor-promoting phorbol diester or with platelet-derived growth factor caused the phosphorylation of the transferrin receptor by protein kinase C (Ca2+/phospholipid-dependent enzyme) at serine 24 and increased the cell surface expression of the transferrin receptor. The hypothesis that the regulation of transferrin receptor cycling by protein kinase C is causally related to the phosphorylation of the receptor at serine 24 was critically tested. Site-directed mutagenesis of the human transferrin receptor cDNA was used to substitute serine 24 with threonine or alanine residues in order to create phosphorylation defective receptors. Wild-type and mutated transferrin receptors were expressed in Swiss 3T3 fibroblasts using the retrovirus vector pZipNeoSV (X). These receptors were functionally active and caused the receptor-mediated endocytosis of diferric transferrin. Incubation of the fibroblasts with phorbol diester caused the phosphorylation of the wild-type (Ser-24) human transferrin receptor, but this treatment did not result in the phosphorylation of the mutated (Ala-24 and Thr-24) receptors. The cycling of the phosphorylation defective receptors was regulated by phorbol diester and platelet-derived growth factor in a manner similar to that observed for the wild-type receptor. We conclude that the regulation of transferrin receptor cycling by protein kinase C is independent of receptor phosphorylation at serine 24 in Swiss 3T3 fibroblasts.</p>
dc.identifier.submissionpathoapubs/904
dc.contributor.departmentDepartment of Biochemistry
dc.source.pages16041-7


This item appears in the following Collection(s)

Show simple item record