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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 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...
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 Nucleolus02:55

The Nucleolus

The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
Necrosis01:16

Necrosis

Necrosis is considered as an “accidental” or unexpected form of cell death that ends in cell lysis. The first noticeable mention of “necrosis” was in 1859 when Rudolf Virchow used this term to describe advanced tissue breakdown in his compilation titled “Cell Pathology”.
Morphological Manifestations of Necrosis
Necrotic cells show different types of morphological appearance depending on the type of tissue and infection. In coagulative necrosis, cells become anucleated and die, but their...

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Updated: May 23, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization
09:31

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

Functional consequences of necdin nucleocytoplasmic localization.

Anat Lavi-Itzkovitz1, Marianna Tcherpakov, Zehava Levy

  • 1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.

Plos One
|March 24, 2012
PubMed
Summary

Necdin, a nervous system protein, moves between the nucleus and cytoplasm via multiple pathways. Disrupting its nuclear entry causes cell death, highlighting necdin

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Last Updated: May 23, 2026

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Necdin is a MAGE family protein predominantly expressed in the nervous system.
  • Its interactions with nuclear and cytoplasmic proteins are known, but its transport mechanism remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of necdin's nucleocytoplasmic transport.
  • To identify proteins involved in necdin's localization and function.

Main Methods:

  • A large-scale yeast RRS interaction screen using necdin as bait.
  • Integration of interaction data to build a comprehensive protein network.
  • Validation of key interactions and characterization of necdin's transport motif.

Main Results:

  • Over 60 new direct binding candidates for necdin were identified.
  • Coherent interaction modules were revealed in the cytoplasm, nucleus, and involved in nucleocytoplasmic transport.
  • Necdin utilizes transportins 1 and 2 for nucleocytoplasmic transport, with a specific motif modulating karyopherin interaction.
  • A necdin mutant (D234P) showed enhanced binding to transportin1 and importin β1.
  • Exclusion of necdin from the nucleus led to significant cell death.

Conclusions:

  • Necdin plays multiple roles in protein complexes across different subcellular compartments.
  • Necdin employs multiple karyopherin-dependent pathways to regulate its localization.
  • Nucleocytoplasmic transport of necdin is critical for cell survival.