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Updated: Jul 10, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 27, 2011

Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway

C Lamaze1, A Dujeancourt, T Baba

  • 1Unité de Biologie des Interactions Cellulaires, URA CNRS 1960, Institut Pasteur, Paris, France. clamaze@pasteur.fr

Molecular Cell
|July 21, 2001
PubMed

Insights

Clathrin-dependent endocytosis is not the only pathway for receptor internalization. Interleukin 2 (IL2) receptors use a clathrin-independent endocytosis route in lymphocytes, requiring dynamin and Rho GTPases.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Transmembrane receptor internalization is crucial for cellular signaling and regulation.
  • Clathrin-dependent endocytosis has been considered the primary mechanism for receptor uptake.

Purpose of the Study:

  • To investigate alternative endocytosis pathways for transmembrane receptors.
  • To determine the mechanism of interleukin 2 (IL2) receptor internalization in lymphocytes.

Main Methods:

  • Selective inhibition of clathrin-dependent endocytosis using dominant-negative Eps15 mutants.
  • Ultrastructural and biochemical analyses of IL2 receptor trafficking.
  • Investigating the role of dynamin and Rho family GTPases.

Main Results:

  • Blocking clathrin-mediated endocytosis did not affect IL2 receptor uptake.
  • IL2 receptors are internalized via a constitutive clathrin-independent pathway in lymphocytes.
  • This pathway is associated with detergent-resistant membrane domains and requires dynamin and Rho GTPases.

Conclusions:

  • Receptor-mediated endocytosis is more diverse than previously thought.
  • The IL2 receptor utilizes a distinct clathrin-independent endocytosis mechanism in lymphocytes.

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