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Related Experiment Videos

Dab2 links CIN85 with clathrin-mediated receptor internalization.

Katarzyna Kowanetz1, Janos Terzic, Ivan Dikic

  • 1Ludwig Institute for Cancer Research, Husargatan 3, Uppsala 75124, Sweden.

FEBS Letters
|November 5, 2003
PubMed
Summary

CIN85 scaffold protein binds disabled-2 (Dab2) to regulate receptor tyrosine kinase endocytosis. Growth factor signaling dynamically alters this interaction, influencing protein recruitment during cellular processes.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • CIN85 is a multidomain scaffold protein crucial for downregulating receptor tyrosine kinases (RTKs).
  • Disabled-2 (Dab2) is an endocytic adaptor molecule involved in clathrin-coat assembly.
  • Understanding the interplay between CIN85 and Dab2 is key to elucidating RTK endocytosis regulation.

Purpose of the Study:

  • To investigate the association between CIN85 and Dab2 in mammalian cells.
  • To determine the role of this interaction in the recruitment of Dab2 to the clathrin coat.
  • To explore how growth factor stimulation modulates the CIN85-Dab2 interaction and subsequent endocytic events.

Main Methods:

  • Co-immunoprecipitation assays to confirm protein-protein interactions.

Related Experiment Videos

  • Peptide binding assays using SH3 domains of CIN85 and carboxyl-terminal peptides of Dab2.
  • Analysis of protein localization and dissociation upon growth factor stimulation.

    • Main Results:

    • CIN85 associates with Dab2 in mammalian cells, with all three SH3 domains of CIN85 binding to a specific peptide in Dab2's carboxyl-terminus.
    • CIN85 binding to Dab2 is essential for Dab2 recruitment to the clathrin coat.
    • Growth factor stimulation induces dissociation of Dab2 and clathrin from CIN85, allowing Cbl to bind to CIN85.

    Conclusions:

    • A dynamic interplay exists between CIN85 and its effectors, including Dab2, during receptor tyrosine kinase endocytosis.
    • Growth factor signaling provides a regulatory mechanism for the CIN85-Dab2 interaction, controlling endocytic complex assembly.
    • This dynamic interaction is critical for the efficient downregulation of receptor tyrosine kinases.