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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 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...
Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall of a...

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Related Experiment Video

Updated: Jun 28, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Novel Nucleus-Oriented Quenched Activity-Based Probes Link Cathepsin Nuclear Localization with Mitosis.

Karin Reut Shannon1, Tommy Weiss-Sadan1, Emmanuelle Merquiol1

  • 1The Institute for Drug Research, The School of Pharmacy, The Faculty of Medicine, The Hebrew University, POB 12271, Jerusalem 9112001, Israel.

ACS Sensors
|February 17, 2025
PubMed
Summary

New probes reveal nuclear cysteine cathepsin activity surges before cell division. These tools help understand protease roles in cell cycle progression and cancer development.

Keywords:
cell-cyclecell-penetrating peptidesimaging probesmitosisnuclear cathepsinquenched-activity-based-probes

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Last Updated: Jun 28, 2026

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Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Cysteine cathepsins are proteases often upregulated in diseases like cancer.
  • While typically endolysosomal, cathepsins also localize to the nucleus and influence the cell cycle.
  • Investigating nuclear cathepsin function requires specific tools.

Purpose of the Study:

  • To develop novel tools for studying nuclear cathepsin activity.
  • To explore the role of cathepsins in cell cycle progression.

Main Methods:

  • Design and synthesis of nucleus-directed quenched activity-based probes (qABPs) using cell-penetrating peptides (CPPs).
  • Biochemical validation of CPP-qABPs for potency and selectivity.
  • Application of qABPs in cell fractionation, multimodal flow cytometry-imaging, and time-lapse microscopy in living cells.

Main Results:

  • CPP-qABPs demonstrated potent and selective activity.
  • Confirmed nuclear cathepsin activity in living cells using various imaging techniques.
  • Observed a distinct spatiotemporal pattern: a surge in nuclear cathepsin activity preceding mitosis.

Conclusions:

  • Nuclear-directed qABPs are effective tools for real-time monitoring of nuclear cathepsin activity.
  • The findings suggest previously unrecognized roles for cathepsins in cell division.
  • These probes can advance research into protease involvement in cell division and cancer.