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Updated: May 14, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
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Protein s-nitrosylation measurement.

Yu Qin1, Anindya Dey, Yehia Daaka

  • 1Department of Urology and Prostate Disease Center, University of Florida College of Medicine, Gainesville, Florida, USA.

Methods in Enzymology
|February 5, 2013
PubMed
Summary
This summary is machine-generated.

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G protein-coupled receptors (GPCRs) are regulated by posttranslational modifications like S-nitrosylation. This review details methods for detecting S-nitrosylation, aiding research on GPCR signaling.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • G protein-coupled receptors (GPCRs) are crucial cell surface receptors.
  • Posttranslational modifications, primarily phosphorylation, regulate GPCR signal duration and amplitude.
  • Emerging evidence indicates GPCRs and their effectors undergo S-nitrosylation.

Purpose of the Study:

  • To review current methods for detecting protein S-nitrosylation.
  • To highlight advancements in overcoming technical limitations in S-nitrosylation measurement.
  • To focus on the biotin switch technique and related methodologies.

Main Methods:

  • Protein S-nitrosylation involves covalent attachment of a nitric oxide (NO) group to cysteine residues.
  • Detection methods typically involve cleaving the S-NO bond.

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  • Subsequent detection of reduced thiols or released NO groups is employed.

    • Main Results:

    • Technical challenges in measuring biologic S-nitrosylation have been significantly reduced.
    • The biotin switch technique is a prominent method for S-nitrosylation detection.
    • Related methods also facilitate the study of S-nitrosylation.

    Conclusions:

    • Accurate detection of protein S-nitrosylation is becoming more accessible.
    • Improved methods will advance understanding of GPCR regulation by S-nitrosylation.
    • This review provides a resource for researchers studying S-nitrosylation in biological systems.