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Related Concept Videos

Nuclear Export of mRNA02:31

Nuclear Export of mRNA

Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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...
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 Export of mRNA02:31

Nuclear Export of mRNA

Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...

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Related Experiment Video

Updated: Jul 1, 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

Karyopherins and nuclear import.

Y M Chook1, G Blobel

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. rosenchook@earthlink.net

Current Opinion in Structural Biology
|December 26, 2001
PubMed
Summary
This summary is machine-generated.

New crystal structures reveal how karyopherins (nuclear transport proteins) interact with nuclear localization signals and the nuclear pore complex, advancing our understanding of molecular import mechanisms.

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Last Updated: Jul 1, 2026

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

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Published on: March 11, 2011

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

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Published on: December 10, 2015

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

Published on: May 3, 2018

Area of Science:

  • Molecular biology
  • Structural biology
  • Cell biology

Background:

  • Karyopherin alpha and beta proteins are crucial for nucleocytoplasmic transport.
  • Understanding their structure is key to deciphering nuclear import processes.

Purpose of the Study:

  • To elucidate the molecular mechanisms of nuclear import.
  • To provide structural insights into karyopherin-mediated transport.

Main Methods:

  • X-ray crystallography was used to determine the structures of various karyopherin complexes.
  • Complexes studied include karyopherin alpha with NLS peptides, karyopherin beta2 with Ran, and karyopherin beta1 with substrates, Ran, and nucleoporins.

Main Results:

  • Crystal structures of key karyopherin complexes have been solved.
  • These structures detail interactions involved in nuclear import.

Conclusions:

  • The solved karyopherin structures offer significant insights into the molecular mechanisms of nuclear import.
  • Understanding substrate recognition, GTPase-mediated release, and NPC interactions is enhanced by these structural findings.