Jove
Visualize
Contact Us

Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.5K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
2.5K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

8.5K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.5K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

11.1K
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...
11.1K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

10.9K
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...
10.9K

You might also read

Related Articles

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

Sort by
Same author

Phospholipase D1 and phosphatidic acid are required for MVE fusion and exosome secretion.

Biophysical journal·2026
Same author

Membrane fusion and budding.

Biophysical journal·2025
Same author

Phospholipase D1 produces phosphatidic acid at sites of secretory vesicle docking and fusion.

Molecular biology of the cell·2023
Same author

Membrane dynamics are slowed for Alexa594-labeled membrane proteins due to substrate interactions.

BBA advances·2023
Same author

Biochemically prepared C-reactive protein conformational states differentially affect C1q binding.

BBA advances·2023
Same author

Exosome secretion kinetics are controlled by temperature.

Biophysical journal·2023
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
Same journal

Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.

Biophysical journal·2026
Same journal

Dynamic conformations of fluorophores on self-labeling protein tags.

Biophysical journal·2026
Same journal

Different actions of RyR2 open and closed channel block explained by a multiscale Ca<sup>2+</sup> release model.

Biophysical journal·2026
Same journal

Membrane Environment Sets the Functional pK<sub>a</sub> of Ionizable Lipids.

Biophysical journal·2026
See all related articles
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 Experiment Video

Updated: Jul 5, 2025

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
06:45

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal

Published on: January 14, 2018

8.5K

Syntaxin clusters and cholesterol affect the mobility of Syntaxin1a.

Alan W Weisgerber1, Zdeněk Otruba1, Michelle K Knowles1

  • 1Department of Chemistry and Biochemistry, University of Denver, Denver, Colorado.

Biophysical Journal
|January 15, 2024
PubMed
Summary
This summary is machine-generated.

Syntaxin1a (Syx1a) clusters are crucial for exocytosis. This study reveals Syx1a molecules move more freely within these nanodomains, a mobility dependent on cholesterol and the N-terminal Habc domain for proper cell function.

More Related Videos

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

9.6K
Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

8.0K

Related Experiment Videos

Last Updated: Jul 5, 2025

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
06:45

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal

Published on: January 14, 2018

8.5K
Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

9.6K
Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

8.0K

Area of Science:

  • Cell Biology
  • Neuroscience
  • Biophysics

Background:

  • Syntaxin1a (Syx1a) is vital for exocytosis in neuroendocrine cells.
  • Syx1a forms nanoscale domains on the plasma membrane, which are essential for vesicle docking but disintegrate during fusion.
  • The dynamic balance of Syx1a molecules within these nanodomains is not fully understood.

Purpose of the Study:

  • To elucidate the dynamics of Syx1a molecules relative to cluster position.
  • To understand how Syx1a clusters maintain their balance and how molecules move within them.
  • To investigate the role of the N-terminal Habc domain and cholesterol in Syx1a dynamics and exocytosis.

Main Methods:

  • Developed a labeling strategy to visualize bulk Syx1a clusters and track single Syx1a molecule trajectories simultaneously on PC12 cells.
  • Tracked single Syx1a molecule movement in relation to cluster positions.
  • Utilized simulations to model Syx1a dynamics within clusters.

Main Results:

  • Syx1a molecules exhibit mobility on the plasma membrane, with higher mobility at cluster centers and reduced mobility at cluster edges.
  • The N-terminal Habc domain and cholesterol are essential for this mobility and proper exocytosis.
  • Simulations support a model of Syx1a clusters maintained by a large cage, with high mobility within a smaller radius.
  • Cholesterol depletion significantly reduces Syx1a mobility within clusters.

Conclusions:

  • Syx1a cluster dynamics are influenced by molecular mobility, with specific roles for the N-terminal Habc domain and cholesterol.
  • A caged diffusion model explains the observed Syx1a dynamics within nanodomains.
  • Plasma membrane fluidity, particularly within Syx1a supramolecular clusters, is critical for exocytosis function.