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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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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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Retroviruses02:33

Retroviruses

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Retroviruses and retrotransposons both insert copies of their genetic elements into the genome of the host cell. Thus, the viral genes are passed on when the host genome is replicated or translated. A typical retroviral DNA sequence contains 3-4 genes that encode the different proteins required for its structural assembly and function as a molecular parasite. This DNA is transcribed into a single mRNA, which is very similar in structure to conventional mRNAs, i.e., it is capped at the 5’...
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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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The Proteasome02:18

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst 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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Retrovirus Life Cycles01:10

Retrovirus Life Cycles

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Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
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ERAD and how viruses exploit it.

Hyewon Byun1, Yongqiang Gou1, Adam Zook1

  • 1Department of Molecular Biosciences, Center for Infectious Diseases and Institute for Cellular and Molecular Biology, The University of Texas at Austin Austin, TX, USA.

Frontiers in Microbiology
|July 30, 2014
PubMed
Summary
This summary is machine-generated.

Endoplasmic reticulum-associated degradation (ERAD) maintains cell integrity by clearing defective proteins. Viruses exploit ERAD for replication and immune evasion.

Keywords:
ERADherpesvirusimmune responsepolyomavirusproteasomal degradationretrotranslocationretrovirusubiquitination

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Virology

Background:

  • Endoplasmic reticulum (ER)-associated degradation (ERAD) is a critical cellular quality control pathway in eukaryotes.
  • ERAD prevents the accumulation of misfolded or misassembled proteins, which is linked to various diseases including neurological disorders, cancer, and infections.
  • The ERAD pathway involves substrate recognition, retrotranslocation across the ER membrane, ubiquitination, and proteasomal degradation.

Purpose of the Study:

  • To review the fundamental mechanisms and components of the ERAD pathway.
  • To explore how viral pathogens manipulate ERAD for their own benefit.
  • To understand the role of ERAD in viral replication and immune system evasion.

Main Methods:

  • Literature review of existing research on ERAD.
  • Analysis of studies detailing viral interactions with the ERAD machinery.
  • Synthesis of information on the functional consequences of ERAD modulation by viruses.

Main Results:

  • ERAD is essential for maintaining proteostasis and cellular health.
  • Viruses have evolved sophisticated strategies to hijack ERAD components.
  • Viral exploitation of ERAD facilitates viral replication and helps viruses evade host immune responses.

Conclusions:

  • ERAD is a vital cellular process with significant implications for health and disease.
  • Understanding viral subversion of ERAD offers insights into viral pathogenesis.
  • Targeting ERAD components could represent a novel therapeutic strategy against viral infections.