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 the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

3.9K
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
3.9K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
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,...
6.4K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

8.7K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
8.7K
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

365
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
365
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

3.4K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.4K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.6K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.6K

You might also read

Related Articles

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

Sort by
Same author

Adipogenin promotes the development of lipid droplets by binding a dodecameric seipin complex.

Science (New York, N.Y.)·2025
Same author

Adipogenin Dictates Adipose Tissue Expansion by Facilitating the Assembly of a Dodecameric Seipin Complex.

bioRxiv : the preprint server for biology·2024
Same author

Editorial: The evolving role of lipid droplets: Advancements and future directions.

Frontiers in cell and developmental biology·2023
Same author

Fatty Acyl Coenzyme A Synthetase Fat1p Regulates Vacuolar Structure and Stationary-Phase Lipophagy in Saccharomyces cerevisiae.

Microbiology spectrum·2023
Same author

Seipin forms a flexible cage at lipid droplet formation sites.

Nature structural & molecular biology·2022
Same author

Seipin: harvesting fat and keeping adipocytes healthy.

Trends in cell biology·2021
Same journal

A pan-vertebrate signaling motif controls the molecular function of intracellular AQP12.

The Journal of cell biology·2026
Same journal

Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.

The Journal of cell biology·2026
Same journal

Recruitment and release of XPG during NER is controlled by pre- and post-incision factors and EXO1.

The Journal of cell biology·2026
Same journal

Meiotic CENP-C supports centromere assembly and kinetochore recruitment in spermatogenesis.

The Journal of cell biology·2026
Same journal

Phosphatidylserine and RhoB connect PI4P and PA metabolism to maintain plasma membrane identity.

The Journal of cell biology·2026
Same journal

PIKfyve influences inter-organelle contacts with lysosomes to modulate the endoplasmic reticulum.

The Journal of cell biology·2026
See all related articles

Related Experiment Video

Updated: Dec 17, 2025

Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis
10:23

Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis

Published on: April 17, 2017

10.5K

Building the lipid droplet assembly complex.

Joel M Goodman1

  • 1Department of Pharmacology, University of Texas Southwestern Medical School, Dallas, TX.

The Journal of Cell Biology
|June 25, 2020
PubMed
Summary
This summary is machine-generated.

Researchers identified seipin/Nem1 as a key protein marking the endoplasmic reticulum sites where lipid droplets form. This finding details the assembly of essential protein complexes involved in lipid droplet biogenesis.

More Related Videos

Isolation of Cellular Lipid Droplets: Two Purification Techniques Starting from Yeast Cells and Human Placentas
09:41

Isolation of Cellular Lipid Droplets: Two Purification Techniques Starting from Yeast Cells and Human Placentas

Published on: April 1, 2014

20.3K
Rapid Lipid Droplet Isolation Protocol Using a Well-established Organelle Isolation Kit
08:43

Rapid Lipid Droplet Isolation Protocol Using a Well-established Organelle Isolation Kit

Published on: April 19, 2019

11.9K

Related Experiment Videos

Last Updated: Dec 17, 2025

Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis
10:23

Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis

Published on: April 17, 2017

10.5K
Isolation of Cellular Lipid Droplets: Two Purification Techniques Starting from Yeast Cells and Human Placentas
09:41

Isolation of Cellular Lipid Droplets: Two Purification Techniques Starting from Yeast Cells and Human Placentas

Published on: April 1, 2014

20.3K
Rapid Lipid Droplet Isolation Protocol Using a Well-established Organelle Isolation Kit
08:43

Rapid Lipid Droplet Isolation Protocol Using a Well-established Organelle Isolation Kit

Published on: April 19, 2019

11.9K

Area of Science:

  • Cell Biology
  • Lipid Metabolism
  • Membrane Biology

Background:

  • Lipid droplets (LDs) are crucial cellular organelles involved in energy storage and signaling.
  • The precise biogenesis sites and protein machinery at the endoplasmic reticulum (ER) for LD formation remain incompletely understood.

Purpose of the Study:

  • To investigate the specific ER subdomain involved in lipid droplet (LD) biogenesis.
  • To elucidate the role of key assembly proteins, including seipin/Nem1, in LD formation.

Main Methods:

  • The study utilized advanced microscopy and biochemical techniques to visualize and analyze protein interactions at the ER.
  • Genetic manipulation was employed to assess the function of seipin/Nem1 in LD assembly.

Main Results:

  • Data indicate that seipin/Nem1 localizes to and marks the specific ER subdomain from which LDs emerge.
  • A detailed working model for the assembly of the protein complex involved in LD biogenesis was proposed.

Conclusions:

  • Seipin/Nem1 plays a critical role in initiating lipid droplet formation at specialized ER sites.
  • Understanding this protein complex assembly provides insights into the regulation of cellular lipid metabolism.