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Related Concept Videos

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GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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Related Experiment Video

Updated: Jun 3, 2026

Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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Published on: September 20, 2011

S-nitrosylation-regulated GPCR signaling.

Yehia Daaka1

  • 1The Department of Microbiology and Immunology, University of California, San Francisco, CA, United States. ydaaka@ufl.edu

Biochimica Et Biophysica Acta
|March 15, 2011
PubMed
Summary
This summary is machine-generated.

G protein-coupled receptors (GPCRs) are key cell surface receptors. Protein S-nitrosylation, a novel modification, fine-tunes GPCR signaling and expression, adding new regulatory controls.

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07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • G protein-coupled receptors (GPCRs) are a vast family of cell surface receptors crucial for signal transduction.
  • They regulate diverse cellular functions including metabolism, growth, and migration.
  • GPCR signaling is modulated by various post-translational modifications like phosphorylation and ubiquitination.

Purpose of the Study:

  • To explore the role of protein S-nitrosylation in regulating GPCR signaling and expression.
  • To highlight S-nitrosylation as a novel regulatory mechanism for GPCRs.

Main Methods:

  • Review of existing literature on GPCRs and post-translational modifications.
  • Analysis of emerging evidence on S-nitrosylation in cellular signaling pathways.

Main Results:

  • GPCRs possess a conserved 7-transmembrane domain structure.
  • Post-translational modifications, including phosphorylation, acylation, and ubiquitination, control GPCR signaling termination and trafficking.
  • Protein S-nitrosylation emerges as a significant post-translational modification that fine-tunes GPCR activity and expression.

Conclusions:

  • S-nitrosylation represents a newly appreciated regulatory mechanism for GPCRs.
  • This modification provides an additional layer of control over the numerous cellular processes mediated by GPCRs.
  • Understanding S-nitrosylation's role is vital for comprehending GPCR system regulation.