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

SNAREs and Membrane Fusion01:43

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 Membrane01:26

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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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.

You might also read

Related Articles

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

Sort by
Same author

Body-plan organizer in comb jellies hints at animal ancestry.

Nature·2026
Same author

Targeting the cell membrane in established and emerging model organisms.

Development (Cambridge, England)·2026
Same author

The 3D architecture of the ctenophore aboral organ and the evolution of complex integrative centers in animals.

Science advances·2026
Same author

Neural connectome of the ctenophore statocyst.

eLife·2026
Same author

Rapid and interpretable protein contact map prediction using a pattern-matching strategy.

Physical biology·2026
Same author

The nascent RNA labelling compound 5-ethynyl uridine (EU) integrates into DNA in some animals.

BMC molecular and cell biology·2025

Related Experiment Video

Updated: Jul 6, 2026

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

Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide.

Pawel Burkhardt1, Douglas A Hattendorf, William I Weis

  • 1Research Group Structural Biochemistry, Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.

The EMBO Journal
|March 14, 2008
PubMed
Summary

Sec1/Munc18-like (SM) proteins regulate vesicular fusion by interacting with SNARE proteins. This study reveals how SM proteins control syntaxin accessibility, influencing SNARE complex formation and vesicular transport.

More Related Videos

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture
10:17

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

Published on: August 2, 2019

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements
08:50

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements

Published on: May 12, 2023

Related Experiment Videos

Last Updated: Jul 6, 2026

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

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture
10:17

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

Published on: August 2, 2019

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements
08:50

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements

Published on: May 12, 2023

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Sec1/Munc18-like (SM) proteins are crucial regulators of vesicular fusion, interacting with SNARE proteins.
  • Observed disparate binding modes of SM proteins with syntaxins, including N-peptide binding and binding to a closed syntaxin conformation.

Purpose of the Study:

  • To investigate the binding interactions between SM proteins and syntaxins, focusing on the role of the syntaxin N-peptide.
  • To elucidate the mechanism by which SM proteins, specifically Munc18a, regulate SNARE complex formation and vesicular transport.

Main Methods:

  • Biochemical assays to analyze protein-protein interactions.
  • Investigated binding affinities between SM proteins (Vps45, Munc18a) and syntaxin N-peptides and full-length syntaxins.
  • Assessed the impact of N-peptide binding on SNARE complex formation.

Main Results:

  • The syntaxin 16 N-peptide binds Vps45, with the rest of syntaxin 16 enhancing this interaction.
  • The syntaxin 1a N-peptide acts as a secondary binding site for Munc18a.
  • Munc18a binding to the syntaxin 1a N-peptide inhibits SNARE complex formation, while N-peptide removal allows syntaxin 1a to bind SNAP-25.

Conclusions:

  • SM proteins, like Munc18a, control the accessibility of syntaxins to their SNARE partners.
  • This regulation by SM proteins is crucial for modulating vesicular fusion.
  • The N-peptide binding mechanism may be a conserved regulatory role for all SM proteins in vesicular transport.