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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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Nuclear Localization Signals and Import01:46

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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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The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
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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 Nucleolus02:55

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The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
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Nuclear LC3 Associates with Slowly Diffusing Complexes that Survey the Nucleolus.

Lewis J Kraft1,2, Pallavi Manral3, Jacob Dowler3

  • 1Chemical and Physical Biology Program, Vanderbilt University, Nashville, TN, USA.

Traffic (Copenhagen, Denmark)
|January 6, 2016
PubMed
Summary

Microtubule-associated protein 1 light chain 3 (LC3) targets the nucleus via specific residues, influencing nucleocytoplasmic transport and nucleolar association. These findings reveal LC3’s nuclear role in high-molecular weight complexes.

Keywords:
FRAPMAP1LC3MudPITautophagydiffusionmass spectrometrynucleo-cytoplasmic transportnucleus

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Microtubule-associated protein 1 light chain 3 (LC3) is crucial for cytoplasmic autophagy.
  • Emerging evidence highlights the functional importance of nuclear LC3.
  • Mechanisms of LC3 nuclear targeting and transport remain poorly understood.

Purpose of the Study:

  • Investigate the role of specific LC3 residues (F52 L53, R68-R70, G120) in nuclear targeting.
  • Elucidate LC3's nucleocytoplasmic transport and association with nuclear components.
  • Identify nuclear LC3-interacting proteins.

Main Methods:

  • Site-directed mutagenesis of LC3 residues.
  • Fluorescence recovery after photobleaching (FRAP) for transport analysis.
  • Mass spectrometry to identify interacting proteins.

Main Results:

  • Residues F52 L53 and R68-70, not G120, regulate nuclear targeting and transport rates.
  • LC3 is enriched in nucleoli, with the triple arginine motif critical for this localization.
  • Candidate nuclear LC3-binding proteins identified include MAP1B, tubulin, and 40S ribosomal proteins.

Conclusions:

  • Specific LC3 residues are key determinants of its nuclear localization and transport.
  • LC3's nucleolar enrichment is mediated by its triple arginine motif.
  • LC3 exists in the nucleus within large complexes, potentially scanning the nucleolus.