Genre
Journal articleDate
1999-08-20Author
Morrione, AndreaPlant, Pamela
Valentinis, Barbara
Staub, Olivier
Kumar, Sharad
Rotin, Daniela
Baserga, Renato
Department
BiologyPermanent link to this record
http://hdl.handle.net/20.500.12613/7108
Metadata
Show full item recordDOI
https://doi.org/10.1074/jbc.274.34.24094Abstract
We 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.Citation
Andrea 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.Citation to related work
ElsevierHas part
Journal of Biological Chemistry, Vol. 274, No. 34ADA compliance
For Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.eduae974a485f413a2113503eed53cd6c53
http://dx.doi.org/10.34944/dspace/7088