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Related Experiment Video

Updated: May 18, 2026

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

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S-nitrosylation inhibits pannexin 1 channel function.

Alexander W Lohman¹, Janelle L Weaver, Marie Billaud

¹Robert M. Berne Cardiovascular Research Center, University of Virginia, Charlottesville, Virginia 22908, USA.

The Journal of Biological Chemistry

|October 4, 2012

Summary

S-nitrosylation of pannexin 1 (Panx1) channels by nitric oxide (NO) donors inhibits channel activity and ATP release. This modification occurs at Cys-40 and Cys-346, impacting vascular function.

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Published on: July 5, 2014

Area of Science:

Biochemistry
Cell Biology
Physiology

Background:

S-nitrosylation is a key post-translational modification regulating protein function.
Pannexin 1 (Panx1) channels are expressed in the vasculature and are influenced by nitric oxide (NO).

Purpose of the Study:

To investigate if pannexin 1 (Panx1) undergoes S-nitrosylation.
To determine the effect of S-nitrosylation on Panx1 channel activity and ATP release.

Main Methods:

Biotin switch assay to detect S-nitrosylation.
Electrophysiology to measure Panx1 channel currents.
Site-directed mutagenesis to identify key cysteine residues.

Main Results:

Nitric oxide (NO) donors S-nitrosylated pannexin 1 (Panx1) in cell models.
S-nitrosylation attenuated Panx1 channel currents and inhibited ATP release.
S-nitrosylation at Cys-40 and Cys-346 was identified as critical for inhibiting Panx1 function.

Conclusions:

Pannexin 1 (Panx1) is regulated by S-nitrosylation at specific cysteine residues (Cys-40 and Cys-346).
This modification inhibits Panx1 channel activity and ATP release, suggesting a role in vascular NO signaling.