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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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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,...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

Updated: Jun 28, 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

Unravelling the nuclear matrix proteome.

Jakob Albrethsen1, Jaco C Knol, Connie R Jimenez

  • 1OncoProteomics Laboratory, CCA 1-60, Department Medical Oncology, VUmc-Cancer Center Amsterdam, De Boelelaan 1117, 1081 HV Amsterdam, The Netherlands.

Journal of Proteomics
|October 30, 2008
PubMed
Summary

The nuclear matrix (NM) model proposes a nuclear scaffold. Further research using proteomics, immunodetection, and microscopy is needed to verify its composition and structure.

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Last Updated: Jun 28, 2026

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
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Published on: November 17, 2019

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Area of Science:

  • Cell Biology
  • Proteomics
  • Biochemistry

Background:

  • The nuclear matrix (NM) model suggests a protein/RNA scaffold within the mammalian nucleus.
  • NM proteins are crucial for nuclear functions and potential cancer biomarkers.
  • The NM proteome is defined by a specific extraction protocol, removing other cellular components.

Purpose of the Study:

  • To advocate for a multidisciplinary approach to validate the NM.
  • To elucidate the molecular composition and structural organization of the NM.
  • To advance the understanding of the NM as a biological entity.

Main Methods:

  • Proteomics for comprehensive protein identification.
  • Immunodetection for specific protein localization.
  • Microscopy for visualizing nuclear matrix structure.

Main Results:

  • The study proposes a combined experimental strategy.
  • Preliminary data suggests the NM is a complex proteinaceous structure.
  • The NM's role in nuclear organization requires further investigation.

Conclusions:

  • The NM requires rigorous verification as a distinct biological entity.
  • Integrated proteomics, immunodetection, and microscopy are essential for NM research.
  • Understanding the NM's composition and structure is key to its functional and biomarker potential.