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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
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Related Experiment Video

Updated: Jun 21, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

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Published on: October 1, 2010

SAP97 regulates Kir2.3 channels by multiple mechanisms.

Karen L Vikstrom1, Ravi Vaidyanathan, Susan Levinsohn

  • 1Department of Pharmacology, State University of New York Upstate Medical University, Syracuse, New York, USA.

American Journal of Physiology. Heart and Circulatory Physiology
|July 28, 2009
PubMed
Summary

Coexpressing the inwardly rectifying potassium channel, Kir2.3, with synapse-associated protein 97 (SAP97) significantly increased Kir2.3 current density. SAP97 enhances Kir2.3 cell surface expression and unitary channel conductance.

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High-throughput Screening for Small-molecule Modulators of Inward Rectifier Potassium Channels
10:07

High-throughput Screening for Small-molecule Modulators of Inward Rectifier Potassium Channels

Published on: January 27, 2013

Area of Science:

  • Molecular biology
  • Cellular physiology
  • Ion channel function

Background:

  • Inwardly rectifying potassium channels (Kir) are crucial for regulating membrane potential.
  • Scaffolding proteins like synapse-associated protein 97 (SAP97) are known to modulate ion channel function.
  • The specific interaction between Kir2.3 and SAP97 and its functional consequences remain to be fully elucidated.

Purpose of the Study:

  • To investigate the impact of coexpressing the Kir2.3 channel with SAP97.
  • To determine the mechanisms underlying SAP97-mediated changes in Kir2.3 channel activity.
  • To analyze alterations in cell surface expression, unitary conductance, and open probability.

Main Methods:

  • Coexpression of Kir2.3 and SAP97 in HEK293 cells.
  • Electrophysiological recordings (whole-cell and single-channel).
  • Confocal microscopy for assessing protein localization.

Main Results:

  • Coexpression led to an approximate twofold increase in Kir2.3 current density.
  • SAP97 induced a redistribution of Kir2.3 to the plasma membrane.
  • Single-channel conductance of Kir2.3 showed a significant increase, with peaks at 16, 29, and 42 pS, compared to ~13 pS without SAP97.
  • Channel open probability and rectification properties remained unchanged.

Conclusions:

  • SAP97 association enhances Kir2.3 cell surface expression and unitary channel conductance.
  • Increased single-channel conductance is the primary driver of enhanced whole-cell currents.
  • SAP97 likely binds to the Kir2.3 COOH-terminal domain, altering channel conformation.