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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
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Cell death is an essential process where the body gets rid of old or damaged cells. Cell proliferation and death need to be balanced, as an imbalance between the two may lead to cancer or autoimmune diseases.
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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
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Golgi disintegration and functional disruption during paraptosis.

Xiang Cui1, Liao Yang2, Huali Zhang2

  • 1Health Management Center, The First Affiliated Hospital of Guilin Medical University, Guilin, 541000, China.

Journal of Cell Science
|April 13, 2026
PubMed
Summary

Paraptosis involves new structures called paraptosomes that form as the Golgi apparatus breaks down. This Golgi disintegration is an early event in paraptosis, impacting cell function.

Keywords:
Golgi disintegrationNon-apoptotic cell deathOrganelle stressParaptosisParaptosomeVesicle trafficking

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Paraptosis is a programmed cell death pathway marked by cytoplasmic vacuolation, ER dilation, and mitochondrial swelling.
  • The role of the Golgi apparatus in paraptosis has been poorly understood.

Purpose of the Study:

  • To investigate the involvement of the Golgi apparatus in paraptosis.
  • To characterize novel structures observed during paraptosis.

Main Methods:

  • Treatment of human glioblastoma U251MG cells with paraptosis inducers.
  • Microscopy and biochemical analyses to study cellular structures and protein processing.

Main Results:

  • Identification of paraptosomes, high-density spherical structures, during paraptosis.
  • Paraptosome formation correlated with Golgi apparatus disintegration and fragmentation.
  • Golgi fragmentation preceded endoplasmic reticulum dilation.
  • Impaired secretory function and altered expression of Golgi stress markers were observed.
  • Processing and nuclear translocation of ER stress transducers OASIS and ATF6 were disrupted, with accumulation in paraptosomes.

Conclusions:

  • Paraptosome formation is associated with Golgi disintegration and dysfunction during paraptosis.
  • Golgi remodeling is an early feature of paraptosis, expanding the known morphological characteristics of this cell death process.