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Related Concept Videos

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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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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Clathrin Coated Vesicles01:12

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Protein Translocation Machinery on the ER Membrane01:28

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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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Mitochondrial Protein Sorting01:39

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Related Experiment Video

Updated: Mar 11, 2026

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Structural Mechanism for Cargo Recognition by the Retromer Complex.

María Lucas1, David C Gershlick2, Ander Vidaurrazaga1

  • 1Structural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain.

Cell
|November 28, 2016
PubMed
Summary
This summary is machine-generated.

Retromer protein complex dysfunction is linked to neurodegenerative diseases. This study reveals how retromer recognizes cargo, a crucial step for cellular recycling and understanding disease mechanisms.

Keywords:
cargo recognitionendocytic recyclingendosomesmembrane recruitmentmembrane tubulesprotein coatsretrograde transportretromersorting nexinssorting signals

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Neuroscience

Background:

  • Retromer is a vital multi-protein complex responsible for recycling transmembrane proteins.
  • Dysfunctional retromer is implicated in Alzheimer's and Parkinson's diseases.
  • Mechanisms of retromer cargo recognition and endosomal recruitment remain unclear.

Purpose of the Study:

  • To elucidate the structural basis of retromer cargo recognition and membrane recruitment.
  • To investigate the interaction between retromer subunits, SNX3, and cargo.

Main Methods:

  • X-ray crystallography was employed to analyze a four-component complex.
  • The complex included VPS26, VPS35, SNX3, and a DMT1-II recycling signal.

Main Results:

  • A novel binding site for recycling signals was identified at the VPS26-SNX3 interface.
  • Cooperative interactions among retromer subunits, SNX3, and cargo were revealed.
  • These interactions link cargo signal recognition to membrane recruitment.

Conclusions:

  • The study provides structural insights into retromer's cargo recognition mechanism.
  • Understanding these interactions is crucial for addressing retromer dysfunction in disease.
  • This work lays the foundation for future therapeutic strategies targeting retromer.