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Related Concept Videos

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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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

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.
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Nuclear Export of mRNA02:31

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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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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy
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ESCRT-III controls nuclear envelope reformation.

Yolanda Olmos1, Lorna Hodgson2, Judith Mantell3

  • 1Division of Cancer Studies, Section of Cell Biology and Imaging, King's College London, London SE1 1UL, UK.

Nature
|June 5, 2015
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Summary
This summary is machine-generated.

The endosomal sorting complex required for transport-III (ESCRT-III) machinery is crucial for nuclear envelope reformation during cell division. This study reveals ESCRT-III

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Nuclear envelope (NE) reformation is essential for proper cell division during telophase.
  • This process involves chromatin coating by endoplasmic reticulum-derived membrane and a critical annular fusion step for sealing the envelope.
  • The precise mechanism of annular fusion, particularly the involvement of the p97 AAA-ATPase complex, remains largely unknown.

Purpose of the Study:

  • To investigate the molecular machinery responsible for the annular fusion step during nuclear envelope reformation.
  • To determine the role of the endosomal sorting complex required for transport-III (ESCRT-III) in post-mitotic nuclear envelope sealing.
  • To explore the relationship between ESCRT-III, the p97 complex, and membrane fusion events in cell division.

Main Methods:

  • Immunofluorescence microscopy to visualize the localization of ESCRT-III components at the forming nuclear envelope in human cells.
  • Depletion studies using siRNA or other methods to assess the necessity of ESCRT-III components for nuclear envelope reformation.
  • Co-immunoprecipitation assays to investigate interactions between ESCRT-III components (e.g., CHMP2A, CHMP4B) and p97 complex members (e.g., UFD1).

Main Results:

  • The ESCRT-III machinery was found to localize to sites of annular fusion during nuclear envelope reformation in human cells.
  • Depletion of ESCRT-III components, such as CHMP2A, impaired proper post-mitotic nucleo-cytoplasmic compartmentalization, highlighting its necessity.
  • CHMP2A localization to the forming NE was dependent on CHMP4B, and its function is essential for NE reformation, with p97 complex member UFD1 also being required for localization.
  • These findings suggest a conserved mechanism for membrane remodeling during cell division.

Conclusions:

  • The ESCRT-III machinery plays a novel and essential role in the annular fusion step of nuclear envelope reformation during cell division.
  • The study demonstrates a functional conservation between membrane fusion events in nuclear envelope sealing and cytokinesis abscission.
  • These findings provide new insights into the molecular mechanisms governing cell division and nuclear organization.