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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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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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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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Related Experiment Video

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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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Why do SARS-CoV-2 NSPs rush to the ER?

Maryline Santerre1, Sterling P Arjona2, Charles Ns Allen2

  • 1Molecular Studies of Neurodegenerative Diseases Lab, Lewis Katz School of Medicine, Fels Institute for Cancer Research, Temple University, 3307 North Broad Street, Philadelphia, PA, 19140, USA. tue86122@temple.edu.

Journal of Neurology
|September 2, 2020
PubMed
Summary

SARS-CoV-2 disrupts the central nervous system by rearranging intracellular membranes. This review examines non-structural proteins (NSPs) 3, 4, and 6, highlighting their role in neurodegeneration and potential drug targets.

Keywords:
COVID-19Double-membrane vesicleEndoplasmic reticulum stressGolgi apparatus fragmentationSARS-CoV-2

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Area of Science:

  • Virology
  • Neuroscience
  • Cell Biology

Background:

  • Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) caused the 2020 pandemic, leading to Coronavirus Disease 2019 (COVID-19).
  • SARS-CoV-2 exhibits a tropism for the central nervous system (CNS), impacting neurological functions.
  • Viral non-structural proteins (NSPs) are crucial for viral replication, transcription, and immune evasion.

Purpose of the Study:

  • To review the specific roles of SARS-CoV-2 non-structural proteins (NSPs) 3, 4, and 6.
  • To evaluate their function in intracellular membrane rearrangement and endoplasmic reticulum (ER) stress induction.
  • To assess the potential for these NSPs to cause central nervous system disruption and neurodegeneration.

Main Methods:

  • Literature review focusing on NSPs 3, 4, and 6.
  • Analysis of mechanisms involving viral hijacking of the endoplasmic reticulum (ER) membrane.
  • Evaluation of studies linking viral proteins to neuronal disturbance and neurodegeneration.

Main Results:

  • NSPs 3, 4, and 6 are key players in SARS-CoV-2-induced intracellular membrane rearrangement.
  • Viral manipulation of the ER membrane leads to ER stress and subsequent neuronal disturbance.
  • These NSPs contribute to the virus's ability to establish the replication and transcription complex (RTC).

Conclusions:

  • NSPs 3, 4, and 6 are critical for viral pathogenesis, particularly in CNS involvement.
  • Understanding these NSPs' functions in membrane rearrangement is vital for comprehending neurodegeneration.
  • Targeting these specific NSPs may lead to the development of novel antiviral therapies for neurological complications.