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

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,...
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...
Valence Bond Theory02:42

Valence Bond Theory

Coordination compounds and complexes exhibit different colors, geometries, and magnetic behavior, depending on the metal atom/ion and ligands from which they are composed. In an attempt to explain the bonding and structure of coordination complexes, Linus Pauling proposed the valence bond theory, or VBT, using the concepts of hybridization and the overlapping of the atomic orbitals. According to VBT, the central metal atom or ion (Lewis acid) hybridizes to provide empty orbitals of suitable...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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

Guide to dynamic OCT data analysis.

Biomedical optics express·2025
Same author

Killer toxin K28 resistance in yeast relies on COG complex-mediated trafficking of the defence factor Ktd1.

Journal of cell science·2025
Same author

Wastewater dataset on the SARS-CoV-2 sublineages circulating in Central Arkansas, USA, post-COVID-19 pandemic.

Scientific data·2025
Same author

Intracellular protein crystallization in living insect cells.

FEBS open bio·2025
Same author

Acute GARP Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and O-Glycosylation.

Traffic (Copenhagen, Denmark)·2025
Same author

Transcriptomics as a predictor of biopharmaceutically favourable glycan profiles.

Frontiers in cell and developmental biology·2025
Same journal

Sub1 contributes to heart failure with preserved ejection fraction driven by aging in mice.

Nature communications·2026
Same journal

The BRCA1-A complex restricts replication fork reversal-dependent DNA repair in ATM deficient cells.

Nature communications·2026
Same journal

Signaling downstream of tumor-stroma interaction regulates mucinous colorectal adenocarcinoma apicobasal polarity.

Nature communications·2026
Same journal

Click-polymerized polyenamine membranes for efficient lithium extraction.

Nature communications·2026
Same journal

Joint trajectories of brain atrophy, white matter hyperintensities and cognition quantify brain maintenance.

Nature communications·2026
Same journal

Proton shuttling at electrochemical interfaces under alkaline hydrogen evolution.

Nature communications·2026
See all related articles

Related Experiment Video

Updated: May 13, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
10:31

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay

Published on: January 20, 2015

COG complexes form spatial landmarks for distinct SNARE complexes.

Rose Willett1, Tetyana Kudlyk, Irina Pokrovskaya

  • 1Department of Physiology and Biophysics, UAMS, Little Rock, Arkansas 72205, USA.

Nature Communications
|March 7, 2013
PubMed
Summary
This summary is machine-generated.

The conserved oligomeric Golgi (COG) complex interacts with Golgi SNAREs, revealing COG subunits

More Related Videos

Recording Spatially Restricted Oscillations in the Hippocampus of Behaving Mice
07:10

Recording Spatially Restricted Oscillations in the Hippocampus of Behaving Mice

Published on: July 1, 2018

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

Related Experiment Videos

Last Updated: May 13, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
10:31

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay

Published on: January 20, 2015

Recording Spatially Restricted Oscillations in the Hippocampus of Behaving Mice
07:10

Recording Spatially Restricted Oscillations in the Hippocampus of Behaving Mice

Published on: July 1, 2018

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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Intracellular membrane trafficking relies on vesicular tethers and SNAREs.
  • The conserved oligomeric Golgi (COG) complex is known to tether retrograde intra-Golgi vesicles.

Purpose of the Study:

  • To investigate the interaction between COG complex subunits and Golgi SNAREs.
  • To elucidate the role of COG sub-complexes in defining vesicular sorting specificity within the Golgi.

Main Methods:

  • Yeast two-hybrid assays.
  • Co-immunoprecipitation experiments.
  • COG-based mitochondrial relocalization assays.

Main Results:

  • Three COG subunits (COG4, 6, and 8) interact with specific Golgi SNAREs (STX5, STX6, STX16, GS27, and SNAP29).
  • COG8-STX16 and COG4-STX5 interactions initiate distinct tethering platforms.
  • These platforms facilitate the redirection of Golgi transport intermediates to the mitochondria.

Conclusions:

  • COG sub-complexes play a crucial role in the specificity of vesicular sorting within the Golgi.
  • This interaction provides a novel mechanism for regulating Golgi transport pathways.