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 Localization Signals and Import01:46

Nuclear Localization Signals and Import

6.0K
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...
6.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
Regulation of Nuclear Protein Sorting01:45

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
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.7K
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...
4.7K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K
Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

3.4K
Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
3.4K

You might also read

Related Articles

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

Sort by
Same author

Unfolding Behavior and Conformational Changes Under Different Denaturing Conditions of MAPK 1 (MEK1).

Biomolecules·2026
Same author

Copper-Collagen Interactions Regulate the Mechanical and Invasive Properties of Tumor Spheroids.

Advanced healthcare materials·2026
Same author

Unveiling nuclear localization signals in human arginine deiminase proteins.

Protein science : a publication of the Protein Society·2026
Same author

The intrinsically disordered protein NUPR1 binds to phospholipids.

Protein science : a publication of the Protein Society·2025
Same author

A Review of Silica-Based Nanoplatforms for Anticancer Cargo Delivery.

International journal of molecular sciences·2025
Same author

The Pattern of Copper Release in Copper-Based Nanoparticles Regulates Tumor Proliferation and Invasiveness in 3D Culture Models.

Small science·2025

Related Experiment Video

Updated: Sep 10, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.0K

Importin α3 Is Tolerant to Nuclear Localization Signal Chirality.

Felipe Hornos1, Bruno Rizzuti2,3, José L Neira1,3

  • 1IDIBE, Instituto de investigación, Desarrollo e Innovación en Biotecnologia Sanitaria de Elche, Universidad Miguel Hernández, 03202 Elche, Alicante, Spain.

International Journal of Molecular Sciences
|August 28, 2025
PubMed
Summary

The stereochemistry of nuclear localization signals (NLSs) does not affect their binding to importin proteins. This finding is crucial for understanding nuclear protein import in eukaryotic cells.

Keywords:
D-enantiomersbindingcalorimetrydisordered peptidesfluorescencemolecular simulationsnuclear localization signal

More Related Videos

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.0K
Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.6K

Related Experiment Videos

Last Updated: Sep 10, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.0K
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.0K
Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.6K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear translocation is essential for eukaryotic cell function, involving carrier proteins like importins.
  • Importin α3 (Impα3) binds to nuclear localization signals (NLSs) on proteins.
  • Truncated importin species (∆Impα3) also bind NLSs, lacking the importin binding domain.

Purpose of the Study:

  • To investigate the binding of D-enantiomer NLSs to Impα3 and ∆Impα3.
  • To determine if stereoisomerism impacts NLS binding affinity and location.
  • To explore the role of conformational disorder in NLS-importin interactions.

Main Methods:

  • Nuclear magnetic resonance (NMR) for characterizing NLS structure.
  • Fluorescence, biolayer interferometry (BLI), and isothermal titration calorimetry (ITC) for binding assays.
  • Molecular simulations to analyze binding interactions.

Main Results:

  • D-enantiomer NLSs are monomeric and disordered, similar to L-enantiomers.
  • Binding affinities of D-enantiomer NLSs were comparable to their L-isomer counterparts.
  • Binding occurred at the major NLS binding site on both Impα3 and ∆Impα3.

Conclusions:

  • Stereoisomeric form of NLSs is not critical for binding to importins.
  • The primary structure of the NLS binding site on importin is well-defined.
  • These findings clarify the molecular basis of nuclear protein import.