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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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The Unfolded Protein Response01:37

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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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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The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
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A Wounded Nucleus Needs ESCRT Service.

Rosemarie Ungricht1, Ulrike Kutay1

  • 1Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland.

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Summary
This summary is machine-generated.

Cell migration through small spaces frequently ruptures the nuclear envelope. The ESCRT-III machinery repairs these nuclear envelope wounds, preventing DNA damage and cell death.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Genetics

Background:

  • Cell migration is crucial for development and disease.
  • The nuclear envelope protects the genome but can be damaged during migration.
  • Efficient repair mechanisms are vital for cell survival.

Purpose of the Study:

  • Investigate nuclear envelope ruptures during cell migration.
  • Identify the molecular machinery responsible for repairing nuclear envelope damage.
  • Understand the consequences of unrepaired nuclear envelope damage.

Main Methods:

  • Utilized live-cell imaging to observe nuclear envelope dynamics during migration.
  • Employed genetic and biochemical approaches to study the ESCRT-III machinery.
  • Assessed DNA integrity and cell viability following nuclear envelope damage.

Main Results:

  • Cell migration through narrow constrictions frequently causes nuclear envelope ruptures.
  • The ESCRT-III machinery is essential for sealing nuclear envelope wounds.
  • Impaired ESCRT-III function leads to increased DNA damage and cell death.

Conclusions:

  • Nuclear envelope integrity is vulnerable during cell migration.
  • ESCRT-III plays a critical role in nuclear envelope repair.
  • Targeting ESCRT-III could offer therapeutic strategies for diseases involving cell migration and DNA damage.