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Related Concept Videos

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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The Nucleolus02:55

The Nucleolus

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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 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

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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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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Regulated mRNA Transport02:22

Regulated mRNA Transport

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In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
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Author Spotlight: RNA FISH for Locating lncRNA-SNHG6 in Osteosarcoma Cells
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Src nuclear localization and its prognostic relevance in human osteosarcoma.

Enrica Urciuoli1,2, Ilenia Coletta1, Emanuele Rizzuto3

  • 1Research Laboratories, Bambino Gesù Children's Hospital, Rome, Italy.

Journal of Cellular Physiology
|July 4, 2017
PubMed
Summary

Nuclear Src protein localization is a novel prognostic marker for osteosarcoma patients. Combined detection of nuclear and cytoplasmic Src levels may improve survival prediction and guide therapeutic strategies for this bone cancer.

Keywords:
NMTsSrc tyrosine-kinasemyristoylationosteosarcomaprognosis

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Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Osteosarcoma is a prevalent bone cancer in young individuals.
  • Identifying prognostic markers is crucial for tailoring treatment strategies.
  • The subcellular localization of proteins like Src may offer new insights.

Purpose of the Study:

  • To investigate the prognostic relevance of Src protein's nuclear localization in osteosarcoma.
  • To explore the molecular mechanisms behind Src's variable subcellular distribution.
  • To determine if Src localization can serve as a biomarker for patient survival.

Main Methods:

  • Analysis of Src protein (total and activated pY418) subcellular distribution in 60 osteosarcoma tissue samples using immunohistochemistry.
  • Kaplan-Meier survival analysis to correlate Src localization with overall survival (OS).
  • Investigation of molecular mechanisms using normal osteoblasts and osteosarcoma cell lines, focusing on N-myristoyltransferase enzymes.

Main Results:

  • Variable patterns of total and activated Src expression and localization (nuclear and cytoplasmic) were observed.
  • A correlation was found between Src subcellular localization and osteosarcoma patient overall survival.
  • N-myristoyltransferase enzyme expression and activity correlated with nuclear Src content.

Conclusions:

  • Src protein exhibits previously unrecognized nuclear localization in osteosarcoma cells.
  • Combined assessment of nuclear and cytoplasmic Src levels shows potential as a prognostic marker for osteosarcoma survival.
  • N-myristoyltransferase enzymes are implicated in regulating Src's subcellular localization.