Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

SNAREs and Membrane Fusion

SNAREs and Membrane Fusion

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...

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

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...

Vesicular Tubular Clusters

Vesicular Tubular Clusters

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...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

You might also read

Related Articles

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

Sort by

Same author

Identification and Characterization of an Affimer Affinity Reagent for the Detection of the cAMP Sensor, EPAC1.

Cells·2021

Same author

Feature-based molecular networking for identification of organic micropollutants including metabolites by non-target analysis applied to riverbank filtration.

Analytical and bioanalytical chemistry·2021

Same author

Seeing beyond the limit: A guide to choosing the right super-resolution microscopy technique.

The Journal of biological chemistry·2021

Same author

Simultaneous multi-spectral, single-photon fluorescence imaging using a plasmonic colour filter array.

Journal of biophotonics·2021

Same author

A Role for the Autophagic Receptor, SQSTM1/p62, in Trafficking NF-κB/RelA to Nucleolar Aggresomes.

Molecular cancer research : MCR·2020

Same author

Metabolic Imaging of Urothelial Carcinoma by Simultaneous Autofluorescence Lifetime Imaging (FLIM) of NAD(P)H and FAD.

Clinical genitourinary cancer·2020

Search research articles

Related Experiment Video

Updated: Jul 17, 2026

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

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

Published on: January 14, 2018

Functionally and spatially distinct modes of munc18-syntaxin 1 interaction.

Colin Rickman¹, Claire N Medine, Axel Bergmann

¹Centre for Integrative Physiology, University of Edinburgh, George Square, Edinburgh EH8 9XD, Scotland.

The Journal of Biological Chemistry

|February 1, 2007

Summary

Munc18-1 regulates syntaxin 1a through two distinct binding modes, challenging existing models of membrane trafficking. These interactions occur in different cellular locations, explaining munc18-1

More Related Videos

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Related Experiment Videos

Last Updated: Jul 17, 2026

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

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

Published on: January 14, 2018

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Area of Science:

Molecular Biology
Cell Biology
Neuroscience

Background:

Eukaryotic membrane trafficking relies on SNARE complex formation for membrane fusion.
Syntaxin 1a, a neuronal SNARE protein, is regulated by the Sec1p/munc18 (SM) protein munc18-1.
SM proteins exhibit structural conservation but diverse binding mechanisms and regulatory roles.

Purpose of the Study:

To investigate the binding mechanisms and cellular localization of munc18-1 interaction with syntaxin 1a.
To challenge current models of munc18-1's atypical binding specificity and mode of action.

Main Methods:

In vitro binding assays.
Live-cell imaging techniques.

Main Results:

Munc18-1 interacts with syntaxin 1a via two mechanistically distinct binding modes.
These distinct interactions were observed both in vitro and within living cells.
Functionally divergent interactions occur at separate cellular locations.

Conclusions:

Munc18-1 employs dual, spatially segregated binding modes to regulate syntaxin 1a.
This provides a molecular basis for the multifaceted roles of munc18-1 in membrane trafficking.
Findings revise current understanding of SNARE complex regulation by SM proteins.