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GPCRs Regulate Adenylyl Cylase Activity01:09

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.
Two...
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Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
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GPCR Desensitization

G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

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Related Experiment Video

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Ex Vivo Release of Calcitonin Gene-Related Peptide from the Trigeminovascular System in Rodents
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Published on: May 16, 2022

RAMPs and CGRP receptors.

James Barwell1, Denise Wootten, John Simms

  • 1School of Life and Health Sciences, Aston University, Birmingham, UK.

Advances in Experimental Medicine and Biology
|March 22, 2012
PubMed
Summary

Receptor activity modifying protein 1 (RAMP1) is crucial for cell-surface expression and calcitonin gene-related peptide (CGRP) binding to its receptor. Understanding RAMP1

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Receptor activity modifying protein 1 (RAMP1) forms a complex with calcitonin receptor-like receptor (CLR).
  • This complex serves as the receptor for calcitonin gene-related peptide (CGRP).
  • RAMP1 plays a dual role in facilitating CLR cell-surface expression and CGRP binding.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying RAMP1's function in CLR complex formation and CGRP receptor activity.
  • To identify key residues in RAMP1 involved in CLR interaction and CGRP binding.
  • To investigate the role of RAMP1 in CGRP receptor sensitivity and its physiological relevance.

Main Methods:

  • Structural analysis to predict RAMP1 residues involved in CLR binding (e.g., Y66, F93, H97, F101).

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  • Identification of RAMP1 regions critical for CGRP recognition.
  • Analysis of CLR epitope (residues 23-60) essential for RAMP recognition.
  • Investigating the impact of RAMP1 expression levels on cellular CGRP sensitivity.

    • Main Results:

    • Specific RAMP1 residues (Y66, F93, H97, F101) likely form a binding site for CLR, located near the plasma membrane.
    • Distinct RAMP1 residues are implicated in CGRP recognition, though the exact mechanism remains unclear.
    • Residue W74 in RAMP1 is important for nonpeptide antagonist BIBN4096BS binding but not CGRP binding.
    • A specific epitope on CLR (residues 23-60) is essential for RAMP recognition.

    Conclusions:

    • RAMP1 is essential for both the proper expression and function of the CGRP receptor.
    • Understanding the structural basis of RAMP1-CLR interaction and CGRP binding is key to receptor modulation.
    • Alterations in RAMP1 expression can significantly impact cellular responses to CGRP, highlighting its physiological and pathophysiological importance.