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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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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...
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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.
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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...
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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...
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Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been...
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Fluorescence in situ hybridization, or FISH, was developed in the early 1980s and has quickly become one of the most widely used techniques in cytogenetics. Labeled probes are used to bind complementary DNA or RNA sequences on a chromosome or in a region within a cell. Earlier, the probes could only be obtained by cloning or reverse transcription of a DNA template. Currently, the probe oligonucleotides can be synthesized synthetically. Additionally, with the advancement of optical techniques,...
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Single-Molecule Imaging of Nuclear Transport
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Overlapping nuclear import and export paths unveiled by two-colour MINFLUX.

Abhishek Sau1, Sebastian Schnorrenberg2, Ziqiang Huang2

  • 1Department of Cell Biology and Genetics, Texas A&M University, College Station, TX, USA.

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Nuclear pore transport pathways for import and export occur in overlapping central regions. MINFLUX tracking reveals restricted annular movement within the nuclear pore complex, highlighting its functional divisions.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • The nuclear pore complex (NPC) regulates nucleocytoplasmic exchange, a critical process for cellular function.
  • Visualizing the nanoscale dynamics of macromolecule transport through the NPC at millisecond timescales is challenging.

Purpose of the Study:

  • To visualize the 3D spatiotemporal dynamics of nuclear import and export simultaneously.
  • To investigate the movement and confinement of macromolecules within the NPC's central channel.

Main Methods:

  • Utilized 3D MINFLUX super-resolution microscopy to identify the NPC scaffold.
  • Simultaneously monitored nuclear import and export pathways using high-precision tracking.

Main Results:

  • Demonstrated that both import and export occur in overlapping regions of the NPC's central pore.
  • Identified translocation-arrested import complexes at the pore periphery.
  • Observed translocating complexes confined to a 40-50 nm annulus within the central pore, moving ~1,000-fold slower than in solution and exhibiting pauses.

Conclusions:

  • The NPC permeability barrier is functionally divided into distinct annular rings.
  • Transport within the NPC is highly restricted, involving structural constraints and/or transient binding.
  • 3D MINFLUX tracking offers high spatiotemporal precision with reduced photobleaching for studying molecular transport.