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Related Concept Videos

Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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Nuclear Protein Sorting01:34

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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.
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One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry out specialized functions. Since biological membranes are only selectively permeable to solutes, they help create a compartment with controlled conditions inside an organelle. These microenvironments are tailored to the organelle's specific functions and help isolate them from the surrounding cytosol.
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Nucleosome Remodeling02:54

Nucleosome Remodeling

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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Nuclear Export of mRNA02:31

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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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The Nucleus01:32

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The nucleus is a membrane-bound organelle that acts as a control center in a eukaryotic cell. It contains chromosomal DNA, which controls gene expression and precisely regulates the production of proteins within the cell. In contrast, the DNA inside the mitochondria and chloroplast only carries out functions that are specific to those organelles.
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Author Spotlight: Comprehensive Epigenetic Analysis for Investigating Human Cellular Plasticity and Environmental Adaptation Using Immunofluorescence Assays
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The cellular environment shapes the nuclear pore complex architecture.

Anthony P Schuller1, Matthias Wojtynek2,3, David Mankus4

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.

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|October 14, 2021
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Summary
This summary is machine-generated.

Human nuclear pore complexes (NPCs) are more flexible than previously thought. Cellular environment significantly influences NPC structure and transport channel dimensions.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biophysics

Background:

  • Nuclear pore complexes (NPCs) are essential molecular machines facilitating transport between the nucleus and cytoplasm.
  • NPCs are large structures composed of multiple nucleoporins arranged in distinct rings around a central channel.
  • Understanding NPC structure in its native environment is crucial for comprehending nuclear transport regulation.

Purpose of the Study:

  • To generate a high-resolution structural model of the human NPC within its native cellular environment.
  • To investigate the influence of the cellular context on NPC architecture and dimensions.
  • To explore the functional interdependence of NPC substructures.

Main Methods:

  • Cryo-electron tomography (cryo-ET) of DLD-1 cells.
  • Cryo-focused-ion-beam (cryo-FIB) milling for sample preparation.
  • Targeted degradation of Nup96 to assess ring interdependence.

Main Results:

  • A novel structural model of the human NPC in situ reveals a substantially wider inner ring and a 75% larger central channel volume compared to previous models.
  • Reorganization of nucleoplasmic and cytoplasmic rings was observed, along with membrane asymmetry around the inner ring.
  • Nup96 degradation demonstrated the interdependence of NPC rings in maintaining channel dimensions and membrane asymmetry.

Conclusions:

  • The cellular environment significantly impacts NPC dimensions and architecture, highlighting inherent flexibility.
  • NPC substructures dynamically interact to modulate the central transport channel and membrane asymmetry.
  • This study provides new insights into the plasticity of NPCs in their native cellular context.