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

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

134.0K
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.
134.0K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

6.9K
6.9K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

19.5K
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...
19.5K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

7.4K
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.
GPCRs are also called heptahelical,...
7.4K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

12.4K
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...
12.4K

You might also read

Related Articles

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

Sort by
Same author

Inherent MS-cleavability of diazirine photo-cross-links enables residue-level structural analysis.

Nature communications·2026
Same author

Supramolecular Modulation of Photoinduced Charge Transfer: Tuning Between Tunneling and Incoherent Hopping.

Angewandte Chemie (International ed. in English)·2026
Same author

Mesenchymal stem cell-derived exosomes promote scalp rejuvenation through type XVII collagen regulation via the miR-21-5p/DKK2/Wnt pathway.

Frontiers in cell and developmental biology·2026
Same author

Dynamic Interfacial Evolution and Miscibility of CO<sub>2</sub>-Alkane Systems: The Role of Chain Length.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Unveiling the Dynamic Ionic Interactions at the Single-Molecule Resolution.

Journal of the American Chemical Society·2026
Same author

The Impact of Real-Time Data Analytics on Infection Prevention and Control Practices in Ophthalmology: A Nursing Perspective on Patient Outcomes and Cost-Effectiveness.

Nursing & health sciences·2026

Related Experiment Video

Updated: Mar 26, 2026

Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy
10:24

Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy

Published on: April 9, 2017

11.5K

Specific cell surface labeling of GPCRs using split GFP.

Wen-Xue Jiang1, Xu Dong1, Jing Jiang1

  • 1CAS Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences, Wuhan, Hubei Province 430071, China.

Scientific Reports
|February 10, 2016
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel split green fluorescent protein (GFP) labeling method for G-protein coupled receptors (GPCRs). This technique enables precise visualization of GPCR internalization and function in living cells.

More Related Videos

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

15.9K
Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
10:13

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

Published on: June 9, 2017

17.4K

Related Experiment Videos

Last Updated: Mar 26, 2026

Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy
10:24

Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy

Published on: April 9, 2017

11.5K
Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

15.9K
Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
10:13

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

Published on: June 9, 2017

17.4K

Area of Science:

  • Cell biology
  • Biochemistry
  • Molecular imaging

Background:

  • Specific cell surface labeling is crucial for studying G-protein coupled receptors (GPCRs) internalization and function.
  • Existing methods may lack the speed, specificity, or versatility required for real-time analysis.

Purpose of the Study:

  • To develop a rapid, specific, and versatile labeling scheme for GPCRs on living cell membranes.
  • To enable quantitative assessment of internalized GPCRs using a split fluorescent protein system.

Main Methods:

  • Engineered two β-strands (10 and 11) from superfolder GFP (sfGFP) into extracellular loops of target GPCRs (GPR17 and CysLT2R).
  • Utilized a complementary sfGFP fragment (β-strands 1-9) carrying the mature fluorophore.
  • Exploited the non-fluorescent nature of individual fragments, which become fluorescent upon specific assembly.

Main Results:

  • Demonstrated successful labeling of GPR17 and CysLT2R on the cell surface.
  • Showcased rapid and tight assembly of the split GFP fragments under non-denaturing conditions.
  • Enabled real-time and quantitative assessment of internalized GPCRs.

Conclusions:

  • The developed split GFP labeling scheme is effective for specific and sensitive visualization of GPCRs.
  • This method offers a versatile tool for studying membrane protein dynamics in biological and pharmacological research.
  • The technique facilitates mechanistic insights into GPCR functions and internalization processes.