Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

205
The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
205
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

6.0K
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...
6.0K
GPCR Desensitization01:12

GPCR Desensitization

6.7K
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...
6.7K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.3K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.3K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

6.7K
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
6.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

JPT2/HN1L functions as an NAADP-binding protein in a cell-type-specific manner.

Cell calcium·2026
Same author

Covalent Chemical Tagging of Transmembrane Transport Proteins Illuminates the Internalization Pathways of Xenosiderophores.

Journal of the American Chemical Society·2026
Same author

Nucleotide-Derived Competitive Inhibitors of Ectonucleotidase CD39─A Promising Extracellular Target for Immunotherapy of Cancer.

Journal of medicinal chemistry·2026
Same author

Capturing transient states of heterodimeric ABC transporter TM287/288 by time-resolved small-angle X-ray scattering.

Biophysical journal·2026
Same author

Domain-Specific Agonist Binding Affinities Explain Structural and Functional Regulation of TRPM2.

bioRxiv : the preprint server for biology·2026
Same author

Multiple signaling events are required for NAADP synthesis by DUOX2 and formation of Ca<sup>2+</sup> microdomains to initiate T cell activation.

Science signaling·2026

Related Experiment Video

Updated: Sep 29, 2025

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

3.7K

cADPR Does Not Activate TRPM2.

Winnie Maria Riekehr1, Simon Sander2, Jelena Pick1

  • 1The Calcium Signalling Group, Department of Biochemistry and Molecular Cell Biology, University Medical Centre Hamburg-Eppendorf, 20246 Hamburg, Germany.

International Journal of Molecular Sciences
|March 25, 2022
PubMed
Summary
This summary is machine-generated.

Cyclic ADP-ribose (cADPR) does not activate the TRPM2 channel, contrary to previous suggestions. Adenosine diphosphate ribose (ADPR) is the key activator, binding to specific TRPM2 domains.

Keywords:
calcium signallingcyclic adenosine 5′-diphosphate ribosesecond messengertransient receptor potential channel

More Related Videos

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.1K
A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice
08:35

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

Published on: March 17, 2015

15.0K

Related Experiment Videos

Last Updated: Sep 29, 2025

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

3.7K
Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.1K
A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice
08:35

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

Published on: March 17, 2015

15.0K

Area of Science:

  • Molecular Biology
  • Ion Channel Physiology
  • Biochemistry

Background:

  • Cyclic ADP-ribose (cADPR) is a second messenger involved in calcium release.
  • The role of cADPR in activating the TRPM2 cation channel has been debated for over 15 years.
  • Previous studies reported TRPM2 activation by cADPR, but contamination with ADPR was suspected.

Purpose of the Study:

  • To definitively investigate whether pure cADPR activates the human TRPM2 channel.
  • To clarify the role of ADPR and cADPR in TRPM2 channel function.
  • To re-evaluate conflicting findings regarding cADPR and TRPM2.

Main Methods:

  • Site-directed mutagenesis of TRPM2 N-terminal MHR1/2 and C-terminal NUDT9H domains.
  • Electrophysiological recordings of TRPM2 channel activity.
  • Biochemical assays to assess nucleotide binding to TRPM2 domains.

Main Results:

  • TRPM2 activation by ADPR and 2'-deoxy-ADPR (2dADPR) requires the MHR1/2 and NUDT9H domains.
  • Pure cADPR did not activate TRPM2 under various tested conditions.
  • The cADPR antagonist 8-Br-cADPR inhibited ADPR-mediated TRPM2 activation.
  • ADPR binds to the MHR1/2 domain, whereas cADPR does not.

Conclusions:

  • Pure cADPR does not directly activate the human TRPM2 channel.
  • ADPR, not cADPR, is the direct activator of TRPM2.
  • Specific TRPM2 domains (MHR1/2 and NUDT9H) are crucial for ADPR-mediated channel function.