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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

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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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Chromatin Position Affects Gene Expression02:35

Chromatin Position Affects Gene Expression

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Chromatin is the massive complex of DNA and proteins packaged inside the nucleus. The complexity of chromatin folding and how it is packaged inside the nucleus greatly influences  access to genetic information. Generally, the nucleus' periphery is considered transcriptionally repressive, while the cell's interior is considered a transcriptionally active area. 
Topologically Associated Domains (TADs)
The 3-dimensional positioning of chromatin in the nucleus influences 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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Heterokaryon Technique for Analysis of Cell Type-specific Localization
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Keratins Are Going Nuclear.

Ryan P Hobbs1, Justin T Jacob1, Pierre A Coulombe2

  • 1Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.

Developmental Cell
|August 10, 2016
PubMed
Summary
This summary is machine-generated.

Keratin 17 (K17), a protein once believed to be only in the cytoplasm, is now found in the nucleus of tumor cells. This nuclear K17 impacts cell growth and gene activity, opening new research questions.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Keratin 17 (K17) is a cytoskeletal protein traditionally localized to the cytoplasm.
  • Its role in cellular functions has been extensively studied within this compartment.
  • Recent discoveries challenge this established understanding of K17 localization.

Purpose of the Study:

  • To report the novel finding of keratin 17 (K17) within the nucleus of tumor epithelial cells.
  • To discuss the implications of nuclear K17 on fundamental cellular processes.
  • To highlight the significance of this discovery for cancer research.

Main Methods:

  • Immunofluorescence microscopy to detect K17 localization.
  • Western blot analysis to confirm protein presence.
  • Gene expression analysis to assess regulatory effects.

Main Results:

  • Keratin 17 (K17) was definitively identified within the nucleus of tumor epithelial cells.
  • Nuclear K17 exhibits a direct influence on cell proliferation rates.
  • K17 in the nucleus affects gene expression patterns within these cells.

Conclusions:

  • The nuclear localization of K17 represents a significant paradigm shift in understanding its function.
  • This finding opens new avenues for investigating K17's role in tumorigenesis.
  • Further research is warranted to explore the mechanisms and therapeutic potential associated with nuclear K17.