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

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

19.1K
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
19.1K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.3K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
16.3K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

13.0K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
13.0K

You might also read

Related Articles

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

Sort by
Same author

Structural basis of lipid-dependent allosteric gating mechanisms for PC1-PC2 ion channel.

Nature communications·2026
Same author

Towards the construction of a virtual yeast.

Nature·2026
Same author

CTBPro: A Next-Generation Cholera Toxin Subunit B-Based Neuroanatomical Tracer With Superior Brightness, Stability, and Sensitivity for Enhanced Neural Circuit Mapping.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Structural insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1.

Cell discovery·2026
Same author

Structural insights into human signal peptide peptidase.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

A comprehensive foundation model for cryo-EM image processing.

Nature methods·2025

Related Experiment Video

Updated: Feb 26, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
13:02

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

8.0K

Structure of the Nav1.4-β1 Complex from Electric Eel.

Zhen Yan1, Qiang Zhou1, Lin Wang1

  • 1State Key Laboratory of Membrane Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, China; Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.

Cell
|July 25, 2017
PubMed
Summary

We determined the cryo-EM structure of the electric eel sodium channel (Nav) with its β1 subunit. This reveals how the channel

Keywords:
Na(v) channelsNa(v)1.4cryo-EMelectromechanical couplingfast inactivationstructural biologythe beta-1 subunitvoltage-gated sodium channels

More Related Videos

Visualization of Endosome Dynamics in Living Nerve Terminals with Four-dimensional Fluorescence Imaging
10:51

Visualization of Endosome Dynamics in Living Nerve Terminals with Four-dimensional Fluorescence Imaging

Published on: April 16, 2014

9.5K
Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis
09:52

Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis

Published on: March 12, 2014

12.4K

Related Experiment Videos

Last Updated: Feb 26, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
13:02

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

8.0K
Visualization of Endosome Dynamics in Living Nerve Terminals with Four-dimensional Fluorescence Imaging
10:51

Visualization of Endosome Dynamics in Living Nerve Terminals with Four-dimensional Fluorescence Imaging

Published on: April 16, 2014

9.5K
Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis
09:52

Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis

Published on: March 12, 2014

12.4K

Area of Science:

  • Structural Biology
  • Neuroscience
  • Biophysics

Background:

  • Voltage-gated sodium channels (Nav) are crucial for electrical signaling in excitable cells.
  • Understanding Nav channel structure is key to deciphering action potential generation and propagation.
  • Previous structural studies have provided insights into closed states, but open states remain less understood.

Purpose of the Study:

  • To determine the cryo-electron microscopy (cryo-EM) structure of the electric eel Nav1.4 channel (EeNav1.4) in complex with the β1 subunit.
  • To elucidate the structural basis of channel gating and fast inactivation.
  • To provide insights into the mechanism of action potential propagation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of EeNav1.4 complexed with the β1 subunit.
  • High-resolution structural analysis at 4.0 Å resolution.
  • Comparative structural analysis with previously determined closed Nav channel structures.

Main Results:

  • The cryo-EM structure of EeNav1.4 with the β1 subunit was resolved at 4.0 Å resolution.
  • The β1 subunit's immunoglobulin domain interacts with extracellular loops, and its transmembrane helix contacts voltage-sensing domain III (VSDIII).
  • Voltage-sensing domains are in the 'up' conformation, indicating an open state, with an intracellular gate held open by a digitonin-like molecule.
  • Structural comparisons reveal coupling between gating charge transfer and pore dilation, involving multiple channel segments.
  • The IFM motif, responsible for fast inactivation, is positioned within repeats III and IV, suggesting an allosteric blocking mechanism.

Conclusions:

  • The determined structure provides a high-resolution snapshot of an open state of a voltage-gated sodium channel.
  • The interaction of the β1 subunit influences channel gating and stability.
  • The findings elucidate the mechanism of fast inactivation and pore opening, offering targets for therapeutic interventions.