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Related Experiment Video

Updated: Jul 3, 2026

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

Multiple Kv1.5 targeting to membrane surface microdomains.

Ramón Martínez-Mármol1, Núria Villalonga, Laura Solé

  • 1Molecular Physiology Laboratory, Departament de Bioquímica i Biologia Molecular, Institut de Biomedicina, Universitat de Barcelona, Barcelona, Spain.

Journal of Cellular Physiology
|August 1, 2008
PubMed
Summary
This summary is machine-generated.

Voltage-dependent potassium channels (Kv) are crucial for leukocyte function. Kv1.5 channels primarily localize to non-raft domains in macrophages, but LPS activation can shift them to lipid rafts, influenced by Kv1.5 interactions.

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Last Updated: Jul 3, 2026

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Published on: July 13, 2013

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07:51

Single-Molecule Localization Microscopy of Membrane Proteins using Single-Antibody Labeling

Published on: March 20, 2026

Area of Science:

  • Cell biology
  • Ion channel physiology
  • Membrane biophysics

Background:

  • Surface expression of voltage-dependent potassium channels (Kv) is vital for leukocyte physiology.
  • Lipid rafts are membrane microdomains that concentrate signaling molecules and ion channels.
  • Kv1.3 and Kv1.5 associate to form functional heteromeric channels in macrophages, with distinct stoichiometries potentially altering localization.

Purpose of the Study:

  • To investigate the targeting of heterotetrameric Kv1.5-containing channels to lipid rafts.
  • To determine if Kv1.5 localization is influenced by cellular context and interactions.

Main Methods:

  • Utilized transfected HEK-293 cells, macrophages, L6E9 skeletal myoblasts, heart membranes, and cardiomyocytes.
  • Investigated channel localization using lipid raft association assays (e.g., sucrose density gradient centrifugation).
  • Examined the impact of LPS-induced activation, caveolin co-expression, and Kvbeta2.1 co-expression on Kv1.5 localization.

Main Results:

  • In HEK-293 cells, homo- and heterotetrameric Kv channels targeted to rafts, but Kv1.5 did not target to rafts in macrophages.
  • Kv1.3/Kv1.5 hybrid channels were predominantly found in non-raft microdomains in macrophages.
  • LPS-induced activation shifted Kv1.5 to lipid rafts in macrophages by increasing the Kv1.3/Kv1.5 ratio and caveolin levels.
  • Kv1.5 did not localize to low-buoyancy fractions in skeletal myoblasts or cardiac cells.
  • Co-expression of Cav3(DGV)-mutant confined Kv1.5 to specific vesicles, while Kvbeta2.1 impaired raft targeting in HEK cells.

Conclusions:

  • Kv1.5 localization to lipid rafts is cell-type specific and context-dependent.
  • Partnership interactions of Kv1.5 are key mechanisms governing its targeting to membrane microdomains.
  • Modulation of Kv1.3/Kv1.5 ratio and caveolin expression can alter Kv1.5 raft localization during cellular activation.