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Related Concept Videos

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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Nuclear Protein Sorting01:34

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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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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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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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Expanded polyalanine tracts function as nuclear export signals and promote protein mislocalization via eEF1A1 factor.

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Polyalanine diseases involve protein mislocalization. Targeting eukaryotic translation elongation factor 1 α1 (eEF1A1) may correct this, offering a new therapeutic strategy for these genetic disorders.

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Area of Science:

  • Genetics and Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Polyalanine (poly(A)) diseases arise from expanded GCN triplet repeats, leading to poly(A) tracts in proteins.
  • These expansions cause nuclear proteins, often transcription factors, to mislocalize to the cytoplasm, resulting in transcriptional dysregulation and cellular dysfunction.
  • Nine human disorders, including congenital central hypoventilation syndrome and oculopharyngeal muscular dystrophy, are linked to poly(A) tract expansions.

Purpose of the Study:

  • To identify the mechanisms responsible for the mislocalization of expanded poly(A) proteins.
  • To investigate potential therapeutic targets for poly(A) diseases by understanding protein subcellular localization.
  • To determine the role of interacting partners in the pathogenesis of poly(A) diseases.

Main Methods:

  • Glutathione S-transferase (GST) pulldown assay to identify protein interactions.
  • Mass spectrometry to identify interacting partners of expanded poly(A)-containing proteins.
  • Knockdown of eEF1A1 expression to assess its effect on protein localization and function.

Main Results:

  • Eukaryotic translation elongation factor 1 α1 (eEF1A1) was identified as an interacting partner with expanded poly(A)-containing proteins.
  • Knockdown of eEF1A1 partially corrected the cytoplasmic mislocalization of expanded poly(A) proteins and restored nuclear function.
  • The expanded poly(A) domain was shown to function as a nuclear export signal.

Conclusions:

  • Eukaryotic translation elongation factor 1 α1 (eEF1A1) plays a critical role in regulating the subcellular localization of expanded poly(A) proteins.
  • eEF1A1 represents a potential therapeutic target for treating poly(A) diseases.
  • Understanding the role of eEF1A1 in protein trafficking offers insights into the pathogenesis of these disorders.