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

Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
G Protein-coupled Receptors01:15

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.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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,...
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

You might also read

Related Articles

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

Sort by
Same author

Genomics comes of age: From research tool to routine care.

Journal of internal medicine·2026
Same author

Author Correction: Real-world clinical utility of tumor whole-genome sequencing in solid cancers.

Nature medicine·2026
Same author

Real-world clinical utility of tumor whole-genome sequencing in solid cancers.

Nature medicine·2026
Same author

The RNA-binding protein NOVA-1 regulates circRNA expression, alternative splicing, and aging in Caenorhabditis elegans.

G3 (Bethesda, Md.)·2026
Same author

The RNA-binding protein NOVA-1 regulates circRNA expression, alternative splicing, and aging in <i>C. elegans</i>.

bioRxiv : the preprint server for biology·2025
Same author

Clinical implications of whole genome sequencing in metastatic colorectal cancer.

Oncogene·2025

Related Experiment Video

Updated: Jul 3, 2026

Large-scale Gene Knockdown in C. elegans Using dsRNA Feeding Libraries to Generate Robust Loss-of-function Phenotypes
18:38

Large-scale Gene Knockdown in C. elegans Using dsRNA Feeding Libraries to Generate Robust Loss-of-function Phenotypes

Published on: September 25, 2013

Proteins interacting with Caenorhabditis elegans Galpha subunits.

Edwin Cuppen1, Alexander M van der Linden, Gert Jansen

  • 1Hubrecht Laboratory, Uppsalalaan 8, Utrecht 3584 CT, The Netherlands.

Comparative and Functional Genomics
|July 17, 2008
PubMed
Summary

Researchers identified 11 novel proteins interacting with Caenorhabditis elegans G-protein alpha subunits using yeast two-hybrid screening. These findings reveal new components in G-protein signaling pathways and potential drug targets.

More Related Videos

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
07:22

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

Basic Caenorhabditis elegans Methods: Synchronization and Observation
11:34

Basic Caenorhabditis elegans Methods: Synchronization and Observation

Published on: June 10, 2012

Related Experiment Videos

Last Updated: Jul 3, 2026

Large-scale Gene Knockdown in C. elegans Using dsRNA Feeding Libraries to Generate Robust Loss-of-function Phenotypes
18:38

Large-scale Gene Knockdown in C. elegans Using dsRNA Feeding Libraries to Generate Robust Loss-of-function Phenotypes

Published on: September 25, 2013

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
07:22

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

Basic Caenorhabditis elegans Methods: Synchronization and Observation
11:34

Basic Caenorhabditis elegans Methods: Synchronization and Observation

Published on: June 10, 2012

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Genomics

Background:

  • Heterotrimeric G-protein signaling is crucial for diverse cellular functions.
  • Identifying novel interacting partners of G-protein alpha subunits is essential for understanding signal transduction pathways.
  • The C. elegans genome encodes multiple Galpha subunits, offering a model for studying G-protein interactions.

Purpose of the Study:

  • To discover novel protein interactors of Caenorhabditis elegans Galpha subunits.
  • To characterize the specificity of these interactions with different Galpha subunits and their activation states.
  • To investigate the biological relevance of identified G-protein interactors in vivo.

Main Methods:

  • Large-scale yeast two-hybrid screening was employed to identify protein-protein interactions.
  • Expression pattern analysis and RNA interference (RNAi) were used to assess biological relevance.
  • Membrane recruitment assays were conducted to validate interactions in a living organism.

Main Results:

  • Eleven distinct proteins were identified as interactors of four different C. elegans Galpha subunits.
  • Interactions were specific to particular Galpha subunits and varied with the activation status of the Galpha subunit.
  • Novel interactors include nuclear receptor superfamily members and a haspin homolog, alongside known G-protein interacting proteins.

Conclusions:

  • The study successfully identified novel components of G-protein signaling pathways in C. elegans.
  • The findings provide a foundation for further research into the functional roles of these newly discovered interactors.
  • Specific interactions, such as between GPA-7 and NHR-22, were validated in vivo, highlighting their biological significance.