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

5.8K
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,...
5.8K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.5K
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...
3.5K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.5K
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...
2.5K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

4.7K
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...
4.7K
COP Coated Vesicles00:59

COP Coated Vesicles

7.9K
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
7.9K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.3K

You might also read

Related Articles

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

Sort by
Same author

VPS13C/PARK23 initiates lipid transfer and membrane remodeling for efficient lysosomal repair.

Nature communications·2026
Same author

<i>Siphoviridae</i> phage tails co-enrich with ex vivo amyloids.

bioRxiv : the preprint server for biology·2026
Same author

Atg18 interaction positions Atg2 for efficient lipid transfer into phagophore elongation.

The EMBO journal·2026
Same author

Three-Dimensional Visualization and Proteomic Analysis of Human Cardiac Transthyretin Amyloidosis Tissue Reveals Microangiopathy and Capillary Occlusion.

Journal of the American Heart Association·2026
Same author

Building bridges: BLTP2 forms ER-plasma membrane contact sites.

The Journal of cell biology·2026
Same author

A dual sensor regulates P-glycoprotein's structural plasticity.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jul 15, 2025

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

30.1K

Structure of the ceramide-bound SPOTS complex.

Jan-Hannes Schäfer1, Carolin Körner2, Bianca M Esch2

  • 1Osnabrück University Department of Biology/Chemistry Structural Biology section, 49076, Osnabrück, Germany.

Nature Communications
|October 4, 2023
PubMed
Summary

This study reveals the structure of the serine palmitoyltransferase (SPT) complex, uncovering how ceramide and other molecules regulate sphingolipid production and cellular stress responses.

More Related Videos

Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis
09:09

Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis

Published on: April 27, 2021

2.2K
High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

7.3K

Related Experiment Videos

Last Updated: Jul 15, 2025

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

30.1K
Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis
09:09

Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis

Published on: April 27, 2021

2.2K
High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

7.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Sphingolipids are crucial for cell membrane structure and stress responses.
  • Serine palmitoyltransferase (SPT) controls the rate-limiting step in sphingolipid synthesis.
  • SPT activity is regulated by binding partners like Tsc3, Orm proteins, ceramides, and Sac1.

Purpose of the Study:

  • To elucidate the structural organization and regulatory mechanisms of the yeast SPT complex.
  • To understand how SPT interacts with its regulatory partners, including Tsc3, Orm1, and Sac1.

Main Methods:

  • High-resolution cryo-electron microscopy (cryo-EM) was employed.
  • Structures of the yeast SPT complex with Tsc3 and Orm1 (SPOT) were determined.
  • The structure of a monomeric complex with Sac1 (SPOTS) was also resolved.

Main Results:

  • The structures revealed tight interactions between ceramide, Orm1, and the SPT complex, explaining ceramide-dependent inhibition.
  • Binding sites for ceramide and ergosterol were observed within the SPOTS complex.
  • These findings suggest a co-regulation mechanism linking sphingolipid biogenesis and sterol metabolism.

Conclusions:

  • The study provides the first high-resolution structures of the yeast SPT complex with key regulatory partners.
  • Structural insights clarify the molecular basis of ceramide-mediated inhibition of SPT.
  • The findings reveal a potential link between sphingolipid and sterol metabolism regulation.