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

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Nuclear Export01:42

Nuclear Export

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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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...

You might also read

Related Articles

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

Sort by
Same author

Bottom-up synthesis of molecular nanodiamond from nanographene.

Nature·2026
Same author

Enzyme-Free Phosphorylation with Kinetic Gating in a De Novo Coiled-Coil System.

Journal of the American Chemical Society·2026
Same author

Design of Fuel-Dependent, Complex-Coacervate-Based Synthetic Cells.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Mimicking a Light-Harvesting Complex to Accelerate Photooxidation in Asymmetric Lipid Membrane Nanoreactors.

Angewandte Chemie (International ed. in English)·2026
Same author

Lighting up Polynitrodopamine: from Electropolymerization to Photopatterning of Ultrathin Films.

ACS applied materials & interfaces·2026
Same author

DNA affects the phenotype of fuel-dependent coacervate droplets.

Nature communications·2026
Same journal

Efficient Chirality-Induced Spin Selectivity in Self-Assembled Monolayers of Ru<sub>2</sub><sup>5</sup><sup>+</sup> Paddlewheel Complexes.

Journal of the American Chemical Society·2026
Same journal

Direct Evidence for the Sulfonium-Mediated Photopolymerization of 1,2-Dithiolanes.

Journal of the American Chemical Society·2026
Same journal

Ionic Cluster Catalyst Assembly Strategy for Ethylene Polymerization and Copolymerization.

Journal of the American Chemical Society·2026
Same journal

Gate-Tailoring with Protons and Metal Cations in a Flexible Zeolite for High-Efficiency Ethylene/Ethane Separation.

Journal of the American Chemical Society·2026
Same journal

Pyridyl Radical-Induced Catalytic Reconstruction of Cyclic Sulfides.

Journal of the American Chemical Society·2026
Same journal

Probing Interfaces in Membrane Electrode Assemblies via <i>Operando</i> Infrared Spectroscopy at Model Gas-Liquid-Solid Triple-Phase Boundaries.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.

Maximilian Schuler1,2, Emirhan Koca1,2, Leon Driehaus-Ortiz1

  • 1Max Planck Institute for Polymer Research, Ackermannweg 10, D-55128 Mainz, Germany.

Journal of the American Chemical Society
|June 24, 2026
PubMed
Summary
This summary is machine-generated.

Scientists created synthetic biomolecular condensates using simple peptides and cellular RNA. These dynamic, liquid-like assemblies form reversibly within cells, offering new ways to organize intracellular components.

More Related Videos

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
10:53

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
09:04

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Related Experiment Videos

Last Updated: Jun 25, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
10:53

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
09:04

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Area of Science:

  • Cell Biology
  • Biochemistry
  • Synthetic Biology

Background:

  • Biomolecular condensates are crucial for intracellular organization, formed via liquid-liquid phase separation.
  • Creating synthetic, dynamic compartments within living cells using minimal components is a significant challenge.

Purpose of the Study:

  • To engineer synthetic coacervates within living cells using minimalistic peptides.
  • To investigate the role of endogenous biomolecules in guiding synthetic condensate formation and function.

Main Methods:

  • Design and synthesis of short cationic peptides with targeting motifs.
  • Utilizing complex coacervation principles for in vitro and in vivo studies.
  • Employing cellular RNA and ATP as potential drivers for coacervation.

Main Results:

  • Peptides formed liquid-like coacervates in nucleolar regions, driven by interactions with cellular RNA.
  • RNA was a more potent driver of coacervation than ATP in vitro.
  • The synthetic coacervates exhibited transient and reversible behavior, responding to peptide supply and depletion.

Conclusions:

  • Endogenous biopolymers, particularly RNA, can direct the formation of synthetic coacervates using simple peptides.
  • This approach enables reversible reorganization of intracellular components.
  • Provides a framework for engineering synthetic coacervates with life-like, nonequilibrium features for cellular applications.