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Related Concept Videos

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ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
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Flippase
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Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
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Kv1.5 association modifies Kv1.3 traffic and membrane localization.

Rubén Vicente1, Núria Villalonga, Maria Calvo

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

The Journal of Biological Chemistry
|January 26, 2008
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Potassium channel Kv1.3 and Kv1.5 form hybrid channels that traffic differently to cell membranes. This differential targeting impacts immune cell regulation.

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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

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Profiling Voltage-gated Potassium Channel mRNA Expression in Nigral Neurons using Single-cell RT-PCR Techniques
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Published on: September 27, 2011

Area of Science:

  • Ion channel biophysics
  • Cellular immunology
  • Membrane biology

Background:

  • Potassium channels, specifically Kv1.3 and Kv1.5, are crucial for physiological responses in leukocytes.
  • Channel activity is linked to their association with lipid rafts within the cell membrane.
  • The oligomeric state of ion channels can influence their localization and function.

Purpose of the Study:

  • To investigate the traffic and membrane targeting of heterotetrameric Kv1.3/Kv1.5 channels.
  • To understand how different subunit compositions affect channel surface expression and raft association.
  • To explore the physiological relevance of Kv1.3/Kv1.5 heteromer localization in immune cells.

Main Methods:

  • Heterotetrameric channel formation and surface expression analysis in HEK cells.
  • Förster Resonance Energy Transfer (FRET) and pharmacological assays to confirm functional hybrid channels.
  • Cholesterol depletion, caveolae colocalization, and Fluorescence Recovery After Photobleaching (FRAP) to assess raft association and mobility.
  • Immunoprecipitation and studies in lipopolysaccharide-activated macrophages.

Main Results:

  • Kv1.3 and Kv1.5 form multiple heterotetramers with varying surface expression levels.
  • Functional hybrid Kv1.3/Kv1.5 channels are confirmed, associating with caveolar raft domains.
  • Homomeric Kv1.3 channels show greater association with caveolin traffic compared to heteromers.
  • Hybrid Kv1.3/Kv1.5 channels exhibit higher mobility than Kv1.3 homotetramers, indicating distinct microdomain targeting.
  • Distinct raft targeting mechanisms for Kv1.3 and Kv1.5 were observed in activated macrophages.

Conclusions:

  • Kv1.3/Kv1.5 heteromerization leads to differential membrane targeting and raft association.
  • The localization of Kv1.3/Kv1.5 heteromers is implicated in the regulation of immune cell function.
  • Understanding heteromeric channel traffic provides insights into complex immune system regulation.