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Updated: Sep 28, 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 26, 2011

Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans

Chih-Ying Chen1, Michael L Reese, Peter K Hwang

  • 1Department of Microbiology and Immunology, Graduate Group in Biophysics, The G.W.Hooper Foundation, University of California, San Francisco, CA 94143-0552, USA.

The EMBO Journal
|November 12, 2002
PubMed

Insights

Clathrin light chains (LCa and LCb) interact with clathrin heavy chain (HC) through specific residues, regulating coated vesicle formation. This study reveals structural insights into LC-HC interactions crucial for endocytosis and organelle biogenesis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Clathrin light chain subunits (LCa and LCb) are essential regulators of coated vesicle formation.
  • Coated vesicles mediate protein sorting in receptor-mediated endocytosis and organelle biogenesis.

Purpose of the Study:

  • To characterize the binding interactions between clathrin light chains (LCa and LCb) and clathrin heavy chain (HC).
  • To elucidate the structural basis of LC-HC interaction and its role in clathrin assembly.

Main Methods:

  • Yeast two-hybrid assays to map core interaction domains.
  • Site-directed mutagenesis to identify critical residues involved in binding.
  • Circular dichroism and molecular dynamics to generate a structural model.

Main Results:

  • Core interaction mapped to HC residues 1267-1522 and LCb residues 90-157.
  • Mutations disrupting helix breakers in LCb core abolished HC association.
  • Compensatory mutations in HC rescued binding defects, pinpointing specific contacts.
  • LCa and LCb share similar interaction mechanisms with HC.

Conclusions:

  • LCa and LCb function as alpha-helices interacting along the HC.
  • A structural model of LC-HC interaction provides novel insights into LC control of clathrin assembly.
  • Understanding these interactions is key for regulating endocytosis and organelle biogenesis.

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