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

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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

Protein Translocation Machinery on the ER Membrane

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 translocon complex.
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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 cytoskeletal...
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

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...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...

You might also read

Related Articles

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

Sort by
Same author

Centrosome linker protein CEP68 modulates cellular stress responses via nuclear condensate formation and HSP27 interaction.

iScience·2026
Same author

Dynamic conformational ensembles of soluble Tau encode neuronal toxicity prior to aggregation.

bioRxiv : the preprint server for biology·2026
Same author

LXR agonist rescues synaptic dysfunction and degeneration in SPG3A patient-specific iPSC-derived neurons.

Acta neuropathologica communications·2025
Same author

Small peptide P110 mitigates axonal degeneration of SPG15 patient iPSC-derived neurons by targeting mitochondrial dysfunction.

Neurobiology of disease·2025
Same author

ER shaping closes the gap in wound healing.

Nature cell biology·2025
Same author

Pathway Analyses of Inherited Neuropathies Identify Putative Common Mechanisms of Axon Degeneration.

Annals of clinical and translational neurology·2025

Related Experiment Video

Updated: May 12, 2026

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
07:49

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum

Published on: January 22, 2019

Untangling the web: mechanisms underlying ER network formation.

Uma Goyal1, Craig Blackstone

  • 1National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.

Biochimica Et Biophysica Acta
|April 23, 2013
PubMed
Summary
This summary is machine-generated.

New research reveals proteins that shape the endoplasmic reticulum (ER) architecture, including its tubules and junctions. These proteins are crucial for ER structure and function, particularly in neurons.

Keywords:
AtlastinEndoplasmic reticulumHereditary spastic paraplegiaMorphologyREEPReticulon

More Related Videos

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
16:43

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

Related Experiment Videos

Last Updated: May 12, 2026

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
07:49

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum

Published on: January 22, 2019

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
16:43

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • The endoplasmic reticulum (ER) is a vital organelle with a complex membrane network.
  • While its roles in biosynthesis and transport are well-studied, the mechanisms generating its distinctive architecture are emerging.
  • Understanding ER structure is key to understanding cellular function.

Purpose of the Study:

  • To elucidate the molecular mechanisms and protein families responsible for shaping the endoplasmic reticulum.
  • To explore the roles of specific proteins in forming ER tubules, junctions, and sheets.
  • To investigate the dynamic nature of ER morphology and its implications.

Main Methods:

  • Review of recent findings on ER-shaping proteins.
  • Analysis of protein families like reticulons, REEPs, atlastin, and Lunapark.
  • Examination of cytoskeletal interactions and their impact on ER structure.

Main Results:

  • Proteins with hydrophobic hairpin domains (reticulons, REEPs) shape high-curvature tubules.
  • Dynamin-related GTPases (atlastin family) mediate three-way junction formation.
  • Specific proteins (p180, CLIMP-63) are involved in shaping ER sheets.
  • Cytoskeletal interactions and signaling pathways contribute to dynamic ER shaping.
  • Mutations in ER-shaping proteins are linked to hereditary spastic paraplegia.

Conclusions:

  • A diverse set of proteins, including reticulons, REEPs, and atlastin family members, cooperatively generate the ER's complex architecture.
  • Proper ER morphology is essential for cellular function, especially in neurons, as evidenced by links to hereditary spastic paraplegia.
  • Further research into ER-shaping mechanisms will illuminate fundamental cellular processes and disease pathologies.