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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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Autophagy01:27

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Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
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Delivery Pathways to the Lysosome01:36

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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
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The Proteasome01:13

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
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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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Related Experiment Video

Updated: Oct 6, 2025

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
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Bay41-4109-induced aberrant polymers of hepatitis b capsid proteins are removed via STUB1-promoted p62-mediated

Jiacheng Lin1,2, Limin Yin1, Xia-Zhen Xu1

  • 1Key Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education, Fuzhou, China.

Plos Pathogens
|January 14, 2022
PubMed
Summary
This summary is machine-generated.

The E3 ubiquitin ligase STUB1 removes aberrant hepatitis B virus (HBV) core protein polymers. STUB1 enhances HBV capsid protein allosteric modulator Bay41-4109

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Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Hepatitis B virus (HBV) core protein (HBc) is crucial for viral replication.
  • Heteroaryldihydropyrimidine compounds (HAPs) like Bay41-4109 modulate HBc, inhibiting HBV production.
  • The cellular fate of HAP-induced aberrant HBc polymers remains unclear.

Purpose of the Study:

  • To investigate the cellular mechanisms for clearing HAP-induced aberrant HBc polymers.
  • To explore the role of STUB1 in the degradation of these polymers.
  • To assess the therapeutic potential of enhancing STUB1 levels for HBV treatment.

Main Methods:

  • Utilized HepAD38 cell lines and HBV-infected HepG2-NTCP cells.
  • Employed HBV transgenic mouse models.
  • Investigated protein interactions and cellular degradation pathways, including macroautophagy.

Main Results:

  • Identified STUB1 as essential for removing Bay41-4109-induced aberrant HBc polymers.
  • Demonstrated STUB1 recruits BAG3 for transport to the perinuclear region, initiating p62-mediated macroautophagy and lysosomal degradation.
  • Showed STUB1 overexpression enhances Bay41-4109's inhibition of HBeAg, HBV virions, and cccDNA formation.

Conclusions:

  • STUB1-mediated clearance is critical for the efficacy of HAP-induced aberrant HBc polymer degradation.
  • Elevating STUB1 levels potentiates the antiviral effects of Bay41-4109.
  • Targeting STUB1 offers a promising strategy for developing curative HBV therapies.