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dc.creatorMorrione, Andrea
dc.creatorPlant, Pamela
dc.creatorValentinis, Barbara
dc.creatorStaub, Olivier
dc.creatorKumar, Sharad
dc.creatorRotin, Daniela
dc.creatorBaserga, Renato
dc.date.accessioned2021-11-09T15:40:40Z
dc.date.available2021-11-09T15:40:40Z
dc.date.issued1999-08-20
dc.identifier.citationAndrea Morrione, Pamela Plant, Barbara Valentinis, Olivier Staub, Sharad Kumar, Daniela Rotin, Renato Baserga, mGrb10 Interacts with Nedd4, Journal of Biological Chemistry, Volume 274, Issue 34, 1999, Pages 24094-24099, ISSN 0021 9258, https://doi.org/10.1074/jbc.274.34.24094.
dc.identifier.issn1083-351X
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/7088
dc.identifier.urihttp://hdl.handle.net/20.500.12613/7108
dc.description.abstractWe have utilized the yeast two-hybrid system to identify proteins interacting with mouse Grb10, an adapter protein known to interact with both the insulin and the insulin-like growth factor-I receptors. We have isolated a mouse cDNA clone containing the C2 domain of mouse Nedd4, a ubiquitin protein ligase (E3) that also contains a hect (homologous to the E6-APcarboxyl-terminus) domain and three WW domains. The interaction with Grb10 in the two-hybrid system was confirmed using the full-length Nedd4, and it was abolished by deleting the last 148 amino acids of Grb10, a region that includes the SH2 domain and the newly identified BPS domain. The interaction between Grb10 and Nedd4 was also reproduced in vivo in mouse embryo fibroblasts, where endogenous Nedd4 co-immunoprecipitated constitutively with both the endogenous and an overexpressed Grb10. This interaction was Ca2+-independent. Grb10 interacting with Nedd4 was not ubiquitinated in vivo, raising the possibility that this interaction may be used to target other proteins, like tyrosine kinase receptors, for ubiquitination.
dc.format.extent6 pages
dc.languageEnglish
dc.language.isoeng
dc.relation.ispartofFaculty/ Researcher Works
dc.relation.haspartJournal of Biological Chemistry, Vol. 274, No. 34
dc.relation.isreferencedbyElsevier
dc.rightsAttribution CC BY
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titlemGrb10 Interacts with Nedd4
dc.typeText
dc.type.genreJournal article
dc.description.departmentBiology
dc.relation.doihttps://doi.org/10.1074/jbc.274.34.24094
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.description.schoolcollegeTemple University. College of Science and Technology
dc.creator.orcidMorrione|0000-0002-2319-7884
dc.temple.creatorMorrione, Andrea
refterms.dateFOA2021-11-09T15:40:40Z


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