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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
This summary is machine-generated.

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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.

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.