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Related Concept Videos

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 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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

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Related Experiment Video

Updated: Jun 25, 2026

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
06:23

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

Published on: April 27, 2019

Essential role of nuclear localization for yeast Ulp2 SUMO protease function.

Mary B Kroetz1, Dan Su, Mark Hochstrasser

  • 1Department of Cell Biology, Yale University, New Haven, CT 06520-8114, USA.

Molecular Biology of the Cell
|February 20, 2009
PubMed
Summary

The SUMO protease Ulp2

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • SUMOylation is a reversible post-translational modification crucial for cellular processes.
  • SUMO proteases, like yeast Ulp2 and human SENP6, regulate SUMOylation.
  • Ulp2 is vital for chromosome stability and cell cycle progression in yeast.

Purpose of the Study:

  • To investigate the functional roles of Ulp2's N-terminal domain (NTD) and C-terminal domain (CTD).
  • To determine the requirements for Ulp2's nuclear localization and function.
  • To understand the structural basis for the poor conservation of NTDs in the Ulp2/SENP6 family.

Main Methods:

  • Deletion mutagenesis of Ulp2's CTD and NTD.
  • Analysis of poly-SUMO conjugate accumulation.

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Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80
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Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80

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Reporter-based Growth Assay for Systematic Analysis of Protein Degradation
07:47

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Published on: November 6, 2014

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Last Updated: Jun 25, 2026

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
06:23

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

Published on: April 27, 2019

Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80
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Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80

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Reporter-based Growth Assay for Systematic Analysis of Protein Degradation
07:47

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Published on: November 6, 2014

  • Assessment of nuclear import using beta-importin Kap95.
  • Functional complementation assays with a heterologous NLS.
  • Main Results:

    • CTD deletion moderately impacts yeast growth but increases poly-SUMO conjugates.
    • The NTD is essential for Ulp2 function and nuclear targeting.
    • Specific short sequences within the NTD mediate nuclear localization.
    • Replacing the NTD with a heterologous NLS largely restores Ulp2 function.

    Conclusions:

    • Nuclear localization of Ulp2 is critical for its in vivo function.
    • Minimal regions within the NTD are sufficient for nuclear import.
    • This explains the limited sequence conservation observed in the NTDs of Ulp2/SENP6 family proteases.