Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

mGrb10 interacts with Nedd4.

A Morrione1, P Plant, B Valentinis

  • 1Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. morrion1@jeflin.tju.edu

The Journal of Biological Chemistry
|August 14, 1999
PubMed
Summary

Researchers identified Nedd4, a ubiquitin ligase, interacting with Grb10, an adapter protein. This interaction, confirmed in vivo, suggests Nedd4 may target other proteins for ubiquitination.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The primate-specific Nedd4-1(NE) localizes to late endosomes in response to amino acids to suppress autophagy.

Nature communications·2025
Same author

The College of Radiographers Research Strategy for the next five years.

Radiography (London, England : 1995)·2021
Same author

Intestinal knockout of Nedd4 enhances growth of Apc<sup>min</sup> tumors.

Oncogene·2016
Same author

Clinical aspects and diagnostic relevance of neuroautonomic evaluation in patients with unexplained falls.

Aging clinical and experimental research·2013
Same author

NGR-TNF, a novel vascular-targeting agent, does not induce cytokine recruitment of proangiogenic bone marrow-derived cells.

British journal of cancer·2013
Same author

Chronic nitrate therapy reduces positivity rate of tilt testing potentiated with sublingual nitroglycerin in patients with unexplained syncope.

European journal of internal medicine·2013

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Interactions

Background:

  • Grb10 is an adapter protein that interacts with insulin and insulin-like growth factor-I receptors.
  • Nedd4 is a ubiquitin protein ligase (E3) containing C2, HECT, and WW domains.

Purpose of the Study:

  • To identify proteins interacting with mouse Grb10 using the yeast two-hybrid system.
  • To characterize the interaction between Grb10 and Nedd4.

Main Methods:

  • Yeast two-hybrid system screening.
  • Co-immunoprecipitation in mouse embryo fibroblasts.
  • Analysis of protein interaction domains.

Main Results:

  • A mouse cDNA clone encoding the C2 domain of Nedd4 was isolated.

Related Experiment Videos

  • Full-length Nedd4 was confirmed to interact with Grb10 in a yeast two-hybrid system.
  • The interaction was abolished by deleting the C-terminal 148 amino acids of Grb10, including the SH2 and BPS domains.
  • Endogenous Nedd4 and Grb10 were found to co-immunoprecipitate in vivo in mouse embryo fibroblasts.
  • The interaction between Grb10 and Nedd4 was calcium-independent.
  • Grb10 interacting with Nedd4 was not ubiquitinated in vivo.

    • Conclusions:

    • Grb10 interacts with the ubiquitin ligase Nedd4.
    • This interaction occurs in vivo and is mediated by specific domains of Grb10.
    • The interaction may serve to target other proteins, such as tyrosine kinase receptors, for ubiquitination by Nedd4.