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

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

4.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
4.7K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

10.5K
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...
10.5K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

2.1K
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.
2.1K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

18.1K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
18.1K
Spindle Assembly02:50

Spindle Assembly

3.3K
Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...
3.3K
Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

3.1K
As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall...
3.1K

You might also read

Related Articles

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

Sort by
Same author

TMPRSS2-ERG confers resistance of prostate cancer to antiandrogens.

EMBO molecular medicine·2026
Same author

Illuminating Clinical TEAD Inhibitors Through Structural Biology.

Journal of medicinal chemistry·2026
Same author

FRZB-induced anti-angiogenic effect via Caveolin-1-mediated TGFβ signalling.

Nature communications·2026
Same author

Bridging phenotype and function in bladder cancer using immuno-competent organoids and ex vivo drug screening.

Journal of experimental & clinical cancer research : CR·2026
Same author

The Deubiquitinating Enzyme Otub2 Modulates Pancreatic Beta-Cells Function and Survival.

Frontiers in bioscience (Landmark edition)·2026
Same author

Discovery of Pan-TEAD Inhibitors That Disrupt YAP-TEAD Interaction as a Potential Therapy for Gastric Cancers and Mutant KRAS and EGFR Lung Cancers.

ACS medicinal chemistry letters·2026

Related Experiment Video

Updated: May 7, 2026

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

11.0K

Tethering the assembly of SNARE complexes.

WanJin Hong1, Sima Lev2

  • 1School of Pharmaceutical Sciences, Xiamen University, Xiamen, People's Republic of China; Institute of Molecular and Cell Biology, Singapore.

Trends in Cell Biology
|October 15, 2013
PubMed
Summary

Tethering factors link transport vesicles to target membranes and help assemble soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes. This review explores how tethering factors coordinate vesicle tethering and SNARE-mediated fusion.

Keywords:
SM proteinsSNAREpinSNAREsmembrane fusiontethering factors

More Related Videos

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

10.6K
Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

8.2K

Related Experiment Videos

Last Updated: May 7, 2026

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

11.0K
SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

10.6K
Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

8.2K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Vesicle fusion is essential for intracellular transport and cellular functions.
  • Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex assembly drives membrane fusion.
  • Tethering factors connect vesicles to target membranes before fusion.

Purpose of the Study:

  • To review recent findings on the role of tethering factors in SNARE complex assembly.
  • To understand the coupling mechanism between vesicle tethering and membrane fusion.
  • To highlight the interactions between tethering factors, SNAREs, and Sec1/Munc18 (SM) proteins.

Main Methods:

  • Literature review of recent studies.
  • Analysis of molecular interactions.
  • Summary of experimental evidence.

Main Results:

  • Tethering factors positively regulate SNARE complex assembly.
  • Direct physical interactions link tethering factors, SNAREs, and SM proteins.
  • This coupling ensures specific and functional SNARE complex formation.

Conclusions:

  • Tethering factors play a crucial role in coordinating vesicle tethering and fusion.
  • Understanding these interactions provides insights into intracellular membrane trafficking.
  • Further research on these protein complexes can reveal new therapeutic targets.