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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...
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...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
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...
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...
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

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Related Experiment Video

Updated: May 31, 2026

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
11:19

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

Sorting the nuclear proteome.

Denis C Bauer1, Kai Willadsen, Fabian A Buske

  • 1Queensland Brain Institute, School of Chemistry and Molecular Biosciences, Queensland Facility for Advanced Bioinformatics, The University of Queensland, St Lucia, Australia.

Bioinformatics (Oxford, England)
|June 21, 2011
PubMed
Summary
This summary is machine-generated.

Researchers mapped 3567 mouse nuclear proteins to intra-nuclear compartments using a predictive model. This reveals how proteins associate with compartments, highlighting the role of transcription factors in immune responses coordinated by PML bodies.

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Related Experiment Videos

Last Updated: May 31, 2026

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
11:19

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

Quantitative Analysis of Chromatin Proteomes in Disease
08:11

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Nuclei Isolation from Adult Mouse Kidney for Single-Nucleus RNA-Sequencing
06:00

Nuclei Isolation from Adult Mouse Kidney for Single-Nucleus RNA-Sequencing

Published on: September 20, 2021

Area of Science:

  • Cell Biology
  • Genomics
  • Proteomics

Background:

  • The cell nucleus contains dynamic, membraneless compartments crucial for nuclear events.
  • Understanding protein localization within these compartments is key to nuclear function.
  • Drivers of protein mobility and association remain largely unknown.

Purpose of the Study:

  • To investigate the determinants of protein associations with eight intra-nuclear compartments.
  • To develop a predictive model for mapping intra-nuclear protein organization.
  • To create a comprehensive map of mouse nuclear protein associations.

Main Methods:

  • Integrated protein interaction data, protein domains, post-translational modification sites, and protein sequence data.
  • Developed a predictive model for protein-compartment associations.
  • Utilized genome-wide data and statistical analysis, including false discovery assessment.

Main Results:

  • Achieved a mean AUC of 0.71 in predicting protein-compartment associations.
  • Generated a map of 3567 mouse nuclear proteins and their compartment associations.
  • Identified the collective role of transcription factors within compartments, with PML bodies coordinating immune responses.

Conclusions:

  • The developed model accurately predicts protein localization within nuclear compartments.
  • The study provides a valuable resource for understanding nuclear organization and protein function.
  • Transcription factors play significant roles in compartment-specific functions, particularly in immune regulation by PML bodies.