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Protein Translocation Machinery on the ER Membrane01:28

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Sec61 protein conducting channel
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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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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ER Retrieval Pathway01:45

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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.
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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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Related Experiment Video

Updated: Nov 19, 2025

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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The Retromer Complex: From Genesis to Revelations.

Matthew N J Seaman1

  • 1University of Cambridge, Cambridge Institute for Medical Research, The Keith Peters Building, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK.

Trends in Biochemical Sciences
|February 2, 2021
PubMed
Summary
This summary is machine-generated.

The retromer complex sorts endosomal proteins, crucial for cell function. Its dysfunction is linked to neurodegenerative diseases like Alzheimer's and Parkinson's, making it a therapeutic target.

Keywords:
endosomemembraneneurodegenerative diseaseretromersorting nexintherapeutic targettubules

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Molecular Biology

Background:

  • The retromer complex is essential for endosomal protein sorting.
  • It maintains the localization of membrane proteins within the endocytic system.
  • Retromer dysfunction is implicated in neurodegenerative diseases and pathogen interactions.

Purpose of the Study:

  • To review the history and discoveries of the retromer complex.
  • To elucidate the mechanisms of retromer function in endosomal protein sorting.
  • To highlight retromer as a potential therapeutic target for neurodegenerative diseases.

Main Methods:

  • Literature review of retromer research.
  • Synthesis of historical identification and recent discoveries.
  • Analysis of retromer's role in protein sorting and disease.

Main Results:

  • Retromer's established role in endosomal protein sorting is confirmed.
  • New insights into retromer function and mechanisms have emerged.
  • The link between retromer and neurodegenerative diseases is further solidified.

Conclusions:

  • Retromer is vital for cellular protein trafficking.
  • Understanding retromer is key to addressing neurodegenerative disorders.
  • Retromer represents a promising avenue for therapeutic intervention.