mGrb10 interacts with Nedd4

Détails

ID Serval
serval:BIB_7C04D7B965EE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
mGrb10 interacts with Nedd4
Périodique
Journal of Biological Chemistry
Auteur(s)
Morrione  A., Plant  P., Valentinis  B., Staub  O., Kumar  S., Rotin  D., Baserga  R.
ISSN
0021-9258 (Print)
Statut éditorial
Publié
Date de publication
08/1999
Volume
274
Numéro
34
Pages
24094-9
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Aug 20
Résumé
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-AP carboxyl-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 Ca(2+)-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.
Mots-clé
Animals Calcium/pharmacology Cell Line GRB10 Adaptor Protein Ligases/chemistry/*metabolism Mice Phosphorylation Proteins/chemistry/*metabolism Ubiquitin-Protein Ligases Ubiquitins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 14:03
Dernière modification de la notice
20/08/2019 15:37
Données d'usage