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
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

4.5K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
4.5K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.9K
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...
2.9K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.1K
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...
3.1K
Nuclear Export01:42

Nuclear Export

4.7K
The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
4.7K
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

4.2K
At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
4.2K

You might also read

Related Articles

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

Sort by
Same author

Allosteric disordering of eIF2B regulates the integrated stress response.

Nature chemical biology·2026
Same author

Progerin-induced nuclear envelope remodeling is shaped by cell division and NUP153.

Journal of cell science·2026
Same author

The perijunctional zone is a molecularly distinct muscle subdomain altered in Duchenne muscular dystrophy.

Nature communications·2026
Same author

CDK1 and CEP97 cooperatively control centriole length to orchestrate ciliogenesis and developmental patterning.

Genes & development·2026
Same author

Harnessing viral strategies to reverse cognitive dysfunction through the integrated stress response.

Science (New York, N.Y.)·2026
Same author

COUNTERING AGE-ASSOCIATED ALTERATIONS IN OLIGODENDROCYTE-DERIVED EXTRACELLULAR MATRIX REJUVENATES COGNITION.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Dec 19, 2025

Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange
15:13

Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange

Published on: April 27, 2017

11.4K

LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation.

Alexander von Appen1, Dollie LaJoie2, Isabel E Johnson1

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA.

Nature
|June 5, 2020
PubMed
Summary
This summary is machine-generated.

Nuclear envelope reformation relies on LEM2 protein condensation onto spindle microtubules, activating ESCRT complexes for nuclear sealing and proper cell division. This process is crucial for maintaining nuclear integrity and preventing DNA damage.

More Related Videos

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

3.5K
Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

7.6K

Related Experiment Videos

Last Updated: Dec 19, 2025

Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange
15:13

Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange

Published on: April 27, 2017

11.4K
Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

3.5K
Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

7.6K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Chromatin Dynamics

Background:

  • Nuclear envelope (NE) remodelling is essential for chromosome segregation during cell division.
  • Reformation of sealed nuclei post-mitosis requires endosomal sorting complexes required for transport (ESCRTs) and the transmembrane ESCRT adaptor LEM2.

Purpose of the Study:

  • To elucidate the mechanism by which LEM2 condensation on microtubules regulates ESCRT activation and spindle disassembly.
  • To investigate the role of LEM2's distinct domains in chromatin binding, phase separation, and microtubule interaction.

Main Methods:

  • Investigated LEM2's interaction with BAF, chromatin, and microtubules using biochemical assays.
  • Analyzed LEM2's phase separation properties and its targeting to spindle microtubules.
  • Examined the activation of ESCRT-II/ESCRT-III hybrid protein CHMP7 by LEM2's winged-helix domain.
  • Disrupted LEM2-mediated events in human cells to assess functional consequences.

Main Results:

  • LEM2's LEM motif binds BAF for chromatin association, while its low-complexity domain (LCD) mediates phase separation and microtubule binding.
  • LEM2 condenses onto spindle microtubules, activating CHMP7 to form co-oligomeric rings.
  • Disruption of LEM2 function in human cells impaired ESCRT recruitment, spindle disassembly, and led to nuclear defects and DNA damage.

Conclusions:

  • LEM2 undergoes liquid-like phase separation and co-assembles with CHMP7 to form a crucial 'O-ring seal' at the membrane-chromatin-spindle interface during nuclear reassembly.
  • This mechanism highlights the role of phase separation in coordinating nuclear envelope reformation and spindle disassembly.
  • The findings suggest phase separation contributes to other nuclear envelope functions, including interphase repair and chromatin organization.