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Related Concept Videos

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.
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...
Transducer Mechanism: G Protein–Coupled Receptors01:30

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.
GPCRs are also called heptahelical, 7TM, or...

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Related Experiment Video

Updated: Jul 28, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
11:49

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay

Published on: July 28, 2014

Characterization of a multicomponent receptor for GDNF

J J Treanor1, L Goodman, F de Sauvage

  • 1Department of Neuroscience, Genentech, Inc., South San Francisco, California 94080, USA.

Nature
|July 4, 1996
PubMed
Summary

Glial-cell-line-derived neurotrophic factor (GDNF) requires a novel protein, GDNFR-alpha, for its effects. This protein forms a complex with the Ret receptor, initiating signaling pathways crucial for neuronal survival and development.

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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

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Related Experiment Videos

Last Updated: Jul 28, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
11:49

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay

Published on: July 28, 2014

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

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Glial-cell-line-derived neurotrophic factor (GDNF) is vital for neuronal survival and development.
  • The precise mechanism of GDNF action remained largely unknown.
  • GDNF plays critical roles in the central and peripheral nervous systems, as well as kidney and enteric nervous system development.

Purpose of the Study:

  • To elucidate the molecular mechanism underlying Glial-cell-line-derived neurotrophic factor (GDNF) signaling.
  • To identify the receptor components involved in GDNF-mediated physiological responses.

Main Methods:

  • Characterization of Glial-cell-line-derived neurotrophic factor (GDNF) binding interactions.
  • Investigation of the role of a novel glycosyl-phosphatidylinositol (GPI)-linked protein (GDNFR-alpha) in GDNF signaling.
  • Analysis of the physical association between GDNFR-alpha and the Ret receptor tyrosine kinase.

Main Results:

  • A novel glycosyl-phosphatidylinositol (GPI)-linked protein, GDNFR-alpha, was identified as a high-affinity Glial-cell-line-derived neurotrophic factor (GDNF) binding protein.
  • GDNFR-alpha is expressed on cells responsive to GDNF.
  • Glial-cell-line-derived neurotrophic factor (GDNF) induces the formation of a complex between GDNFR-alpha and the orphan tyrosine kinase receptor Ret, leading to Ret tyrosine phosphorylation.

Conclusions:

  • Glial-cell-line-derived neurotrophic factor (GDNF) utilizes a multi-subunit receptor complex for its signaling.
  • GDNFR-alpha acts as the ligand-binding component, while the Ret receptor functions as the signal-transducing component.