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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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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.
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...
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Regulation of Nuclear Protein Sorting01:45

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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 Export01:42

Nuclear Export

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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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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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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Pinching-off of Coated Vesicles01:32

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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Utilizing the Dyn2 dimerization-zipper as a tool to probe NPC structure and function.

Dirk Flemming1, Philipp Stelter1, Ed Hurt1

  • 1Biochemie-Zentrum der Universität Heidelberg (BZH), Im Neuenheimer Feld, Heidelberg, Germany.

Methods in Cell Biology
|May 27, 2014
PubMed
Summary
This summary is machine-generated.

Dynein light chain 2 (Dyn2) functions as a nucleoporin, enabling in vivo studies of nucleocytoplasmic transport. Its DID-Dyn2 system provides a precise structural label for visualizing protein complexes and modeling nuclear pore structures.

Keywords:
DIDDynein2Electron microscopyFG repeatsLabelNPCNegative stainTransport channel

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Biology

Background:

  • Dynein light chain 2 (Dyn2) was identified as a nucleoporin in yeast.
  • Nucleoporins are crucial for nuclear pore complex (NPC) structure and function.
  • Nucleocytoplasmic transport relies on the intricate organization of NPCs.

Purpose of the Study:

  • To utilize the Dyn2-DID system for probing nucleocytoplasmic transport in vivo.
  • To develop a precise structural label for proteins and protein complexes using Dyn2-DID.
  • To investigate NPC structure and the positioning of subunits within subcomplexes.

Main Methods:

  • Employing the Dyn2-DID system as a molecular tool.
  • Utilizing electron microscopy for visualizing the Dyn2-DID structural label.
  • Analyzing protein complex structures and NPC subcomplex organization.

Main Results:

  • The Dyn2-DID system effectively probes nucleocytoplasmic transport in vivo.
  • A precise structural label was developed, visible via electron microscopy.
  • The label facilitated the identification of subunit positions in NPC subcomplexes.
  • Pseudo-atomic models of large nucleoporins (Nups) were derived.

Conclusions:

  • The Dyn2-DID system is a versatile molecular tool for studying NPC structure and function.
  • Its applications extend beyond the nuclear pore and transport field.
  • This system offers novel insights into protein complex organization and modeling.