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

Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

2.4K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
2.4K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
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,...
6.4K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.3K
Structure of Cadherins01:25

Structure of Cadherins

4.5K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
4.5K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

10.5K
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...
10.5K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

131.2K
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.
131.2K

You might also read

Related Articles

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

Sort by
Same author

CCK+ Interneurons Contribute to Thalamus-Evoked Feed-Forward Inhibition in the Prelimbic Prefrontal Cortex.

The Journal of neuroscience : the official journal of the Society for Neuroscience·2024
Same author

The open gate of the AMPA receptor forms a Ca<sup>2+</sup> binding site critical in regulating ion transport.

Nature structural & molecular biology·2024
Same author

HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.

International journal of molecular sciences·2024
Same author

GSG1L-containing AMPA receptor complexes are defined by their spatiotemporal expression, native interactome and allosteric sites.

Nature communications·2023
Same author

AMPA receptor auxiliary subunit GSG1L suppresses short-term facilitation in corticothalamic synapses and determines seizure susceptibility.

Cell reports·2021
Same author

AMPA Receptor Auxiliary Subunit GSG1L Suppresses Short-Term Facilitation in Corticothalamic Synapses and Determines Seizure Susceptibility.

Cell reports·2020

Related Experiment Video

Updated: Dec 29, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.9K

AMPA receptor structure and auxiliary subunits.

Aichurok Kamalova1,2, Terunaga Nakagawa1,2,3

  • 1Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, Nashville, TN, 37232, USA.

The Journal of Physiology
|February 1, 2020
PubMed
Summary

AMPA-type ionotropic glutamate receptors (AMPARs) mediate fast brain excitation. Auxiliary subunits modulate AMPAR function, impacting learning and memory. Recent structural data reveals molecular insights into these crucial synaptic complexes.

Keywords:
AMPA receptorsAMPA type glutamate receptorsCKAMP44GSG1LShisaSynDIGTARPauxiliary subunitscornichoncryo-electron microscopyelectrophysiologyion channelion channel gating modulationionotropic glutamate receptorsstargazinstructural biologysynaptic plasticitysynaptic transmission

More Related Videos

A High-content Assay for Monitoring AMPA Receptor Trafficking
10:34

A High-content Assay for Monitoring AMPA Receptor Trafficking

Published on: January 28, 2019

7.9K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.5K

Related Experiment Videos

Last Updated: Dec 29, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.9K
A High-content Assay for Monitoring AMPA Receptor Trafficking
10:34

A High-content Assay for Monitoring AMPA Receptor Trafficking

Published on: January 28, 2019

7.9K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.5K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Fast excitatory synaptic transmission in the mammalian brain relies on AMPA-type ionotropic glutamate receptors (AMPARs).
  • AMPAR function is precisely regulated by associated auxiliary subunits, influencing synaptic plasticity and cognitive functions.
  • Understanding these AMPAR-auxiliary subunit complexes is vital for deciphering brain mechanisms of learning and memory.

Purpose of the Study:

  • To review the structural and molecular complexity of AMPAR-auxiliary subunit complexes.
  • To explore the functional diversity of these complexes across different brain regions.
  • To highlight how recent structural insights illuminate the molecular mechanisms of synaptic AMPAR function.

Main Methods:

  • Literature review of structural and functional studies on AMPAR-auxiliary subunit complexes.
  • Analysis of diverse functional modulations provided by different auxiliary subunits.
  • Integration of recent structural data with existing knowledge on synaptic function.

Main Results:

  • AMPARs are modulated by a diverse array of auxiliary subunits, each conferring unique properties.
  • These complexes exhibit significant functional diversity depending on the brain region and subunit composition.
  • Emerging structural information offers unprecedented detail on the molecular interactions within these complexes.

Conclusions:

  • Auxiliary subunits are critical determinants of AMPAR function at the synapse.
  • Structural insights are revolutionizing our understanding of how these complexes operate at a molecular level.
  • Further research into AMPAR-auxiliary subunit complexes holds promise for understanding cognitive processes and neurological disorders.