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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.
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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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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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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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Rapid and Specific Immunomagnetic Isolation of Mouse Primary Oligodendrocytes
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Olig1 Acetylation and Nuclear Export Mediate Oligodendrocyte Development.

Jinxiang Dai1, Kathryn K Bercury1, Weilin Jin2

  • 1Department of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, Colorado 80045.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|December 4, 2015
PubMed
Summary

Oligodendrocyte transcription factor Olig1

Keywords:
Olig1acetylationnuclear export

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Oligodendrocyte transcription factor (Olig1) is crucial for oligodendrocyte development and myelin repair.
  • The mechanism of Olig1 protein's movement between the nucleus and cytoplasm is not fully understood.
  • This translocation is observed during brain development and in conditions like multiple sclerosis.

Purpose of the Study:

  • To elucidate the molecular mechanisms governing Olig1 protein's nuclear-cytoplasmic translocation.
  • To investigate the role of post-translational modifications, specifically acetylation, in regulating Olig1 function.
  • To identify the key regulatory proteins and sequences involved in Olig1 translocation.

Main Methods:

  • Investigated Olig1 acetylation and deacetylation in mouse and rat oligodendrocytes.
  • Identified functional nuclear export sequences (NES) within the Olig1 basic helix-loop-helix domain.
  • Characterized the acetylation site (Lys 150 in human Olig1) within NES1.
  • Assessed the regulation of Olig1 acetylation/deacetylation by CREB-binding protein and specific histone deacetylases (HDAC1, HDAC3, HDAC10).
  • Analyzed the impact of Olig1 acetylation on chromatin association and interaction with inhibitor of DNA binding 2.

Main Results:

  • Olig1 acetylation and deacetylation actively drive its translocation between the nucleus and cytoplasm.
  • Three NES were identified in the basic helix-loop-helix domain, with Lys 150 acetylation site in NES1.
  • CREB-binding protein and HDACs (HDAC1, HDAC3, HDAC10) regulate Olig1 acetylation status.
  • Acetylation reduces Olig1 chromatin binding, enhances interaction with inhibitor of DNA binding 2, and promotes cytoplasmic retention.
  • This acetylation-dependent mechanism is essential for oligodendrocyte maturation.

Conclusions:

  • Olig1 acetylation regulates its dissociation from chromatin and subsequent cytoplasmic translocation.
  • This process is critical for Olig1's role in mature oligodendrocyte function.
  • Understanding Olig1 acetylation provides insights into oligodendrocyte development and diseases involving myelin.