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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Updated: Jun 7, 2026

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
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Published on: April 20, 2015

Design, function and structure of a monomeric ClC transporter.

Janice L Robertson1, Ludmila Kolmakova-Partensky, Christopher Miller

  • 1Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA.

Nature
|November 5, 2010
PubMed
Summary

The ClC (chioride channel) subunit alone functions as the basic unit for transport. This study demonstrates that cross-subunit interactions are not required for Cl(-)/H(+) exchange in ClC transporters.

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Last Updated: Jun 7, 2026

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Membrane Transport

Background:

  • Chloride channel (ClC) proteins facilitate inorganic anion transport for diverse biological functions, including electric fish stunning and cellular acidification.
  • ClC proteins universally adopt a homodimeric structure, with transport machinery localized within each subunit.
  • Previous studies suggested transport cycles reside within individual subunits, but definitive proof was lacking.

Purpose of the Study:

  • To investigate whether the ClC subunit functions independently as the basic unit of transport.
  • To determine if cross-subunit interactions are essential for Cl(-)/H(+) exchange in ClC transporters.

Main Methods:

  • Utilized the known structure of the ClC Cl(-)/H(+) exchanger, ClC-ec1 from Escherichia coli.
  • Designed mutants to destabilize the dimer interface while maintaining subunit structure and transport function.
  • Assessed the transport activity of the engineered monomeric ClC proteins.

Main Results:

  • Successfully generated monomeric ClC proteins by destabilizing the dimer interface.
  • Demonstrated that individual ClC subunits retain their structure and Cl(-)/H(+) exchange function.
  • Confirmed that cross-subunit interactions are not required for the transport activity of ClC transporters.

Conclusions:

  • The ClC subunit is the fundamental functional unit for Cl(-)/H(+) transport.
  • Dimerization is not essential for the catalytic activity of ClC transporters.
  • This finding resolves the debate on whether ClC transporters operate via independent subunits or require inter-subunit cooperation.