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

13.5K
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...
13.5K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

19.4K
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...
19.4K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.4K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
7.4K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.1K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

9.9K
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...
9.9K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.7K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.7K

You might also read

Related Articles

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

Sort by
Same author

Cytopenias and Functional Defects in a Novel Murine Model of VPS45 Severe Congenital Neutropenia.

bioRxiv : the preprint server for biology·2026
Same author

Oncogenic BRAF and KRAS Promote Global DNA Hypomethylation Through a Directed Pathway That Upregulates TET3.

Cancer science·2026
Same author

Nest attendance in two Finnish waterfowl species in relation to per- and polyfluoroalkyl substances and thyroid hormones.

Environmental research·2026
Same author

Differential impacts of wind and waves on albatross flight performance in two ocean basins.

Movement ecology·2025
Same author

Compartmentalized cell envelope biosynthesis in <i>Mycobacterium tuberculosis</i>.

mBio·2025
Same author

Vulnerability of marine megafauna to global at-sea anthropogenic threats.

Conservation biology : the journal of the Society for Conservation Biology·2025

Related Experiment Video

Updated: Apr 1, 2026

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
10:28

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

Published on: December 6, 2019

8.3K

The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes.

Michelle L Dubuke1, Stephanie Maniatis2, Scott A Shaffer2

  • 1Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605.

The Journal of Biological Chemistry
|October 9, 2015
PubMed
Summary

The exocyst complex subunit Sec6 binds SNARE complexes, promoting their assembly rather than inhibiting it. This finding reveals a new role for Sec6 in regulating vesicle fusion during exocytosis.

Keywords:
MSSNARE proteinsexocystexocytosisintracellular traffickingintrinsically disordered proteinprotein cross-linkingprotein-protein interactiontethering complex

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

10.2K
Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

14.5K

Related Experiment Videos

Last Updated: Apr 1, 2026

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
10:28

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

Published on: December 6, 2019

8.3K
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

10.2K
Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

14.5K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Vesicle fusion is crucial for intracellular trafficking in eukaryotic cells.
  • Multisubunit tethering complexes and SNARE complexes are essential for regulated vesicle fusion.
  • The exocyst complex mediates exocytosis, but its interaction with SNAREs is poorly understood.

Purpose of the Study:

  • To investigate the mechanism of exocyst-SNARE interaction in vesicle targeting and fusion.
  • To identify the molecular determinants of the interaction between exocyst subunit Sec6 and SNARE protein Sec9.
  • To elucidate the role of Sec6 in SNARE complex assembly.

Main Methods:

  • In vitro binding assays to study Sec6-Sec9 interaction.
  • Cross-linking and mass spectrometry to map interaction residues.
  • Yeast genetics to assess the functional impact of Sec6 mutations.

Main Results:

  • Sec6 directly binds SNARE proteins Sec9, Sso1, and Snc2.
  • Contrary to the initial hypothesis, Sec6 promotes, not inhibits, SNARE complex assembly.
  • Mutations in identified Sec6 residues lead to yeast growth defects.

Conclusions:

  • Sec6 actively promotes SNARE complex assembly, facilitating vesicle fusion.
  • This study proposes a new model where exocyst subunits facilitate SNARE complex formation.
  • The findings offer insights into the regulation of exocytic vesicle trafficking.