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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 Export of mRNA02:31

Nuclear Export of mRNA

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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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Directionality of Nuclear Transport01:42

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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 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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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.
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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

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Protein dynamics in the nuclear compartment.

Gordon L Hager1, Cem Elbi, Matthias Becker

  • 1Laboratory of Receptor Biology and Gene Expression, Building 41, B602, 41 Library Drive, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5055, USA. hagerg@exchange.nih.gov

Current Opinion in Genetics & Development
|March 15, 2002
PubMed
Summary
This summary is machine-generated.

The classic view of transcriptional initiation complexes is challenged by new findings. Nuclear factors move rapidly, suggesting dynamic interactions rather than stable multi-protein assemblies at regulatory sites.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The traditional model describes transcriptional initiation complexes as stable assemblies stabilized by numerous protein-protein interactions.
  • Recent in vivo studies using protein mobility experiments reveal dynamic behavior of nuclear factors.

Purpose of the Study:

  • To reconcile the classic view of stable initiation complexes with new evidence of dynamic nuclear factor mobility.
  • To explore the implications of rapid factor exchange for understanding gene regulation.

Main Methods:

  • Utilizing live-cell imaging techniques to monitor protein dynamics.
  • Analyzing the mobility and exchange rates of nuclear factors at regulatory sites.

Main Results:

  • Observed rapid movement and quick exchange of many nuclear factors with multiple target sites.
  • Data indicates that nuclear factors do not form permanently stable multi-component complexes.

Conclusions:

  • The classic model of stable transcriptional initiation complexes may be an oversimplification.
  • Dynamic interactions and rapid exchange of factors are crucial for transcriptional regulation, presenting a new paradigm.