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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.
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SNAREs and Membrane Fusion01:43

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Tail-anchoring of Proteins in the ER Membrane01:45

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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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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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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Related Experiment Video

Updated: Jun 6, 2025

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
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Structural basis for Retriever-SNX17 assembly and endosomal sorting.

Amika Singla1, Daniel J Boesch2, Ho Yee Joyce Fung3

  • 1Department of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX, 75390, USA.

Nature Communications
|November 25, 2024
PubMed
Summary
This summary is machine-generated.

Sorting Nexin 17 (SNX17) tethers cargo to the Retriever complex for endosomal recycling. Cargo binding releases SNX17

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Sorting Nexin 17 (SNX17) is crucial for endosomal recycling, mediating cargo protein transport by interacting with the Retriever complex.
  • The precise molecular mechanisms governing the SNX17-Retriever interaction have not been fully elucidated.

Purpose of the Study:

  • To elucidate the structural and biochemical mechanisms of the Sorting Nexin 17 (SNX17)-Retriever complex interaction.
  • To understand how cargo binding regulates SNX17's interaction with Retriever and subsequent endosomal trafficking.

Main Methods:

  • Biochemical assays
  • Cryo-electron microscopy (cryo-EM)
  • Proteomics
  • Cellular imaging

Main Results:

  • SNX17 exists in an autoinhibited state, with its FERM domain binding its C-terminal tail.
  • Cargo binding to SNX17's FERM domain releases the C-terminal tail, which then binds Retriever's VPS35L/VPS26C interface.
  • Disruption of this interface impairs cargo recycling and alters plasma membrane proteome composition.
  • Retriever's binding pocket accommodates other ligands with acidic C-terminal motifs.

Conclusions:

  • A novel mechanism for SNX17-mediated endosomal cargo recycling is revealed, involving cargo-induced release of SNX17's C-terminal tail to bind Retriever.
  • The findings provide structural insights into the SNX17-Retriever interaction and its regulation by cargo.
  • This study highlights Retriever's potential to interact with diverse ligands, impacting cellular trafficking and potentially pathogen interactions.