Related Experiment Video
Updated: Feb 20, 2026

11:05
Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
Published on: February 21, 2019
9.7K
Retromer revisited: Evolving roles for retromer in endosomal sorting
John P Chamberland1, Brigitte Ritter2
1Department of Biochemistry, Boston University School of Medicine, Boston, MA.
The Journal of Cell Biology
|October 25, 2017
Summary
The retromer complex, crucial for endosome to Golgi transport, has functionally diverged. Individual retromer subcomplexes in mammalian cells now organize distinct cargo sorting pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Organelle Biology
Background:
- The retromer complex is a highly conserved protein assembly.
- It is traditionally associated with cargo retrieval from endosomes to the trans-Golgi network.
- Existing models propose a unified function for the retromer complex.
Purpose of the Study:
- To fundamentally question the current retromer model.
- To investigate the functional organization of retromer subcomplexes in mammalian cells.
- To identify distinct sorting pathways mediated by retromer subcomplexes.
Main Methods:
- Utilized advanced cell imaging techniques.
- Employed biochemical assays to analyze protein interactions.
- Investigated retromer function in mammalian cell models.
Main Results:
- Demonstrated functional divergence of individual retromer subcomplexes.
- Identified multiple distinct sorting pathways organized by these subcomplexes.
- Challenged the established model of unified retromer function.
Conclusions:
- Retromer subcomplexes possess specialized roles in intracellular trafficking.
- Mammalian cells utilize functionally distinct retromer subcomplexes for diverse sorting events.
- This finding necessitates a revised understanding of retromer-mediated transport.
Related Concept Videos
The Early Endosome: Endocytosis of Transferrin
4.9K
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...
4.9K
Recycling Endosomes and Transcytosis
3.7K
The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
3.7K
ER Retrieval Pathway
4.9K
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...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
4.9K
Rab Cascades
3.6K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
3.6K
Export of Misfolded Proteins out of the ER
5.3K
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...
5.3K
Maturation of Endosomes
6.0K
The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
The maturing endosome moves along microtubules from the periphery of the cell towards the perinuclear region. This movement of the...
Changes in location
The maturing endosome moves along microtubules from the periphery of the cell towards the perinuclear region. This movement of the...
6.0K

