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Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments
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Intersubunit conformational changes mediate epithelial sodium channel gating.

Daniel M Collier1, Vivian R Tomkovicz1, Zerubbabel J Peterson1

  • 1Department of Internal Medicine and Department of Molecular Physiology and Biophysics, University of Iowa Carver College of Medicine, Iowa City, IA 52242 Department of Internal Medicine and Department of Molecular Physiology and Biophysics, University of Iowa Carver College of Medicine, Iowa City, IA 52242.

The Journal of General Physiology
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PubMed
Summary
This summary is machine-generated.

Interactions between epithelial sodium channel (ENaC) subunits control its gating. Altering these interfaces affects channel activity and responses to physiological signals, revealing a mechanism for sodium homeostasis.

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Area of Science:

  • Physiology
  • Molecular Biology
  • Biophysics

Background:

  • The epithelial sodium channel (ENaC) is vital for sodium absorption in the kidney and lung, regulating blood pressure.
  • Understanding ENaC gating mechanisms is crucial for comprehending sodium homeostasis.

Purpose of the Study:

  • To investigate the role of intersubunit interfaces in controlling ENaC gating.
  • To elucidate the molecular mechanisms underlying ENaC channel activity modulation.

Main Methods:

  • Cysteine substitution and chemical cross-linking to probe intersubunit interfaces.
  • Assessment of ENaC activity, open probability, and responses to pH and sodium via current measurements.
  • Introduction of charged side chains to analyze charge-dependent effects.

Main Results:

  • Identified specific residues at intersubunit interfaces (αK477, βE446, γE455) that interact with adjacent subunits.
  • Demonstrated that cross-linker length influences ENaC current by altering open probability.
  • Showed that interface modifications disrupt gating responses to extracellular pH and sodium.
  • Observed charge-dependent modulation of ENaC activity based on introduced side chains.

Conclusions:

  • Conformational changes at ENaC intersubunit interfaces are critical for channel gating.
  • Increased intersubunit distance favors the open state, while reduced distance favors the closed state.
  • This mechanism allows ENaC activity modulation in response to physiological changes, maintaining sodium balance.