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Related Concept Videos

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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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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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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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Karyopherins regulate nuclear pore complex barrier and transport function.

Larisa E Kapinos1, Binlu Huang1, Chantal Rencurel1

  • 1Biozentrum and the Swiss Nanoscience Institute, University of Basel, Basel, Switzerland.

The Journal of Cell Biology
|September 3, 2017
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Summary
This summary is machine-generated.

Karyopherins (Kaps) regulate nuclear pore complex (NPC) transport and barrier function. Kapα and RanGTP control Kapβ1 dynamics, crucial for cargo release and NPC selectivity.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Nucleocytoplasmic transport relies on karyopherins (Kaps) and a RanGTP gradient.
  • The precise regulation of nuclear pore complex (NPC) barrier selectivity, Kap traffic, and cargo release remains unclear.

Purpose of the Study:

  • To elucidate the coordinated regulation of NPC barrier function, Kap transport, and cargo release.
  • To investigate the role of Kapα in Kapβ1 dynamics and its coupling to NPC barrier properties.

Main Methods:

  • Investigated Kapα and Kapβ1 interactions with FG nucleoporins (FG Nups) and RanGTP.
  • Assessed the impact of Kap depletion and repletion on NPC barrier function.
  • Analyzed the binding affinities of Kap complexes and RanGTP to FG Nups.

Main Results:

  • Kapα enhances Kapβ1 turnover and NPC occupancy in a RanGTP-dependent manner, coupled to cargo release.
  • RanGTP alone is insufficient to release Kapβ1 from NPCs due to binding affinities.
  • Kapα·Kapβ1 depletion abrogates NPC barrier function, while Kapβ1 addition rescues and modulates it.

Conclusions:

  • FG Nups are essential but not sufficient for NPC barrier function.
  • Karyopherins are integral to NPC barrier, transport, and cargo release, operating under Kap-centric control.