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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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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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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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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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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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Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis
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Lipid droplets go nuclear.

Robert V Farese1, Tobias C Walther2

  • 1Department of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Harvard University, Boston, MA 02115 Department of Cell Biology, Harvard Medical School, Harvard University, Boston, MA 02115 Broad Institute of MIT and Harvard, Cambridge, MA 02142 twalther@hsph.harvard.edu robert@hsph.harvard.edu.

The Journal of Cell Biology
|January 6, 2016
PubMed
Summary
This summary is machine-generated.

Lipid droplets (LDs) can form within the cell nucleus. Researchers found that the nuclear membrane, PML-II protein, and promyelocytic leukemia bodies are key to this nuclear LD formation process.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Lipid droplets (LDs) are cytoplasmic organelles involved in lipid metabolism and storage.
  • The presence and function of LDs within the cell nucleus are not well understood.
  • Emerging evidence suggests nuclear LDs may play specific cellular roles.

Purpose of the Study:

  • To investigate the mechanisms and key factors involved in the formation of lipid droplets within the cell nucleus.
  • To explore potential functional relationships between nuclear lipid droplets and other nuclear structures.

Main Methods:

  • Utilized cell imaging techniques to observe nuclear lipid droplet formation.
  • Investigated the role of the nuclear membrane in the process.
  • Examined the involvement of the promyelocytic leukemia protein (PML-II) and promyelocytic leukemia bodies.

Main Results:

  • Demonstrated that lipid droplets can indeed form within the nucleus.
  • Identified the nuclear membrane as a critical component in nuclear LD biogenesis.
  • Showed that the protein PML-II and promyelocytic leukemia bodies are essential for nuclear LD formation.

Conclusions:

  • Nuclear lipid droplet formation is a regulated process involving specific cellular machinery.
  • The nuclear membrane, PML-II, and promyelocytic leukemia bodies are integral to nuclear LD biogenesis.
  • These findings suggest novel functional connections between lipid metabolism and nuclear organization.