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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

6.2K
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...
6.2K
Nuclear Export01:42

Nuclear Export

3.7K
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...
3.7K
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.9K
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...
4.9K
Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

3.9K
Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
3.9K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.5K
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...
2.5K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

3.5K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
3.5K

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Related Experiment Video

Updated: May 6, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

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Stimulated nuclear import by β-like importins.

Karen Flores1, Rony Seger

  • 1Department of Biological Regulation The Weizmann Institute of Science Rehovot 76100 Israel.

F1000Prime Reports
|October 30, 2013
PubMed
Summary

Nuclear shuttling, essential for protein transport, involves canonical importin-α∙β and non-canonical β-like importins. These β-like importins may facilitate rapid nuclear translocation of signaling proteins following cellular stimuli.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Transport

Background:

  • Canonical nuclear shuttling relies on importin-α∙β heterodimers binding nuclear localization signals (NLS) for post-translational protein transport.
  • Non-canonical importins, known as karyopherin-βs or β-like importins, translocate proteins using non-canonical NLS independently of importin-α.
  • The precise mechanisms of β-like importins are less understood but are increasingly linked to stimulated nuclear import.

Purpose of the Study:

  • To investigate the role of β-like importins in protein nuclear translocation.
  • To explore the potential involvement of β-like importins in the rapid, stimulus-induced movement of signaling proteins into the nucleus.

Main Methods:

  • Literature review and synthesis of current research on nuclear import mechanisms.

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Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

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Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
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Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection

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Last Updated: May 6, 2026

Single-Molecule Imaging of Nuclear Transport
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Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
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  • Analysis of studies implicating β-like importins in signal-dependent nuclear translocation.

    • Main Results:

    • β-like importins can mediate nuclear import without importin-α.
    • Emerging evidence suggests β-like importins are involved in the stimulated nuclear translocation of signaling proteins.

    Conclusions:

    • β-like importins represent a distinct pathway for nuclear protein transport.
    • This class of importins may be crucial for the rapid, stimulus-responsive nuclear entry of many proteins.