Related Experiment Video
Updated: Jul 5, 2025

16:43
Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
13.0K
Sculpting nuclear envelope identity from the endoplasmic reticulum during the cell cycle
Pallavi Deolal1,2, Julia Scholz1,2,3, Kaike Ren1,2,3
1Max Perutz Labs, Vienna Biocenter Campus (VBC), Vienna, Austria.
Nucleus (Austin, Tex.)
|January 18, 2024
Summary
The nuclear envelope (NE) disassembles during mitosis and reforms from the endoplasmic reticulum (ER). This review explores NE reformation and how the NE maintains its unique identity and homeostasis distinct from the ER during interphase.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The nuclear envelope (NE) is vital for regulating nuclear functions like transcription and transport.
- The NE shares continuity with the endoplasmic reticulum (ER) but possesses a distinct protein composition.
- During open mitosis, the NE disassembles and must reform to restore nuclear compartmentalization.
Purpose of the Study:
- To review mechanisms of NE reconstitution from the mitotic ER during open mitosis.
- To explore how the NE maintains its unique identity and homeostasis during interphase.
- To highlight the significance of ER-NE membrane junctions.
Main Methods:
- Literature review of existing research on nuclear envelope structure and function.
- Analysis of recent findings on NE-specific lipid metabolism and quality control.
- Examination of endomembrane system dynamics during mitosis and interphase.
Main Results:
- The NE disassembles during open mitosis and reforms from the ER.
- The NE exhibits distinct lipid metabolism and quality control mechanisms compared to the ER.
- Membrane junctions between the ER and NE play a potential role in NE homeostasis.
Conclusions:
- Understanding NE reformation from the ER is key to comprehending nuclear compartmentalization.
- The NE actively maintains its unique identity and homeostasis through specialized mechanisms.
- Further research into ER-NE junctions may reveal novel insights into NE function and regulation.
Related Concept Videos
The Endoplasmic Reticulum
13.7K
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,...
13.7K
Distribution of Cytoplasmic Content
4.1K
Cytokinesis segregates a cell’s chromosomes and organelles into its daughter cells. Organelles divide and grow prior to cell division but cannot be synthesized de novo; therefore, cells must receive at least one copy of each organelle to survive. Currently, many of the details of how the organelles are distributed are not yet fully elucidated.
Distribution of cytoplasmic determinants
The cytoplasm contains various organelles, as well as salts, proteins, and water. The distribution of...
Distribution of cytoplasmic determinants
The cytoplasm contains various organelles, as well as salts, proteins, and water. The distribution of...
4.1K
Assembly of the Lipid Bilayer in the ER
3.2K
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...
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
3.2K
Regulation of Nuclear Protein Sorting
2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
ER Retrieval Pathway
3.8K
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
3.8K
Endoplasmic Reticulum
95.0K
The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
95.0K

