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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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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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Integrated structural analysis of the human nuclear pore complex scaffold.

Khanh Huy Bui1, Alexander von Appen, Amanda L DiGuilio

  • 1European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

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|December 10, 2013
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Summary

The nuclear pore complex (NPC) scaffold

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Area of Science:

  • Cell Biology
  • Structural Biology

Background:

  • The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm in eukaryotic cells.
  • Its large size and complex composition make determining its structure challenging.
  • The overall architecture of the NPC scaffold remains largely unknown.

Purpose of the Study:

  • To determine the structure of the Nup107 subcomplex, a key scaffold motif of the human NPC.
  • To visualize the Nup107 subcomplex in isolation and within the intact NPC.

Main Methods:

  • Integrated approach combining electron tomography, single-particle electron microscopy, and crosslinking mass spectrometry.
  • Structural analysis of the Nup107 subcomplex and its arrangement in the NPC.

Main Results:

  • 32 copies of the Nup107 subcomplex form two reticulated rings within the NPC.
  • These rings are located at the cytoplasmic and nuclear faces of the NPC.
  • This arrangement provides insight into how NPC diameter changes accommodate large cargo transport.

Conclusions:

  • The Nup107 subcomplex forms a dual-ring structure within the NPC scaffold.
  • This structural organization is crucial for the functional adaptability of the NPC.
  • The findings advance our understanding of nucleocytoplasmic transport mechanisms.