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Related Concept Videos

The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
ER Retrieval Pathway01:45

ER Retrieval Pathway

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...
Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...

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Related Experiment Video

Updated: Jun 21, 2026

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells
05:13

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells

Published on: June 30, 2021

Efferocytosis: another function of uPAR.

Francesco Blasi1, Nicolai Sidenius

  • 1Foundation FIRC Institute of Molecular Oncology, Italy.

Blood
|July 25, 2009
PubMed
Summary

The urokinase plasminogen activator receptor (uPAR) influences how macrophages engulf dying neutrophils. Its precise function and mechanism in this process remain complex and debated.

Area of Science:

  • Immunology
  • Cell Biology

Background:

  • The urokinase plasminogen activator receptor (uPAR) is implicated in regulating efferocytosis.
  • Efferocytosis, the clearance of apoptotic cells by phagocytes, is crucial for tissue homeostasis and preventing inflammation.

Discussion:

  • uPAR's role in efferocytosis, specifically the uptake of apoptotic neutrophils by macrophages, is complex.
  • The exact molecular mechanisms by which uPAR influences this process are not fully elucidated and may be subject to controversy.

Key Insights:

  • uPAR acts as a key regulator in the interaction between macrophages and apoptotic neutrophils.
  • Understanding uPAR's function is vital for comprehending efferocytosis dynamics.

Outlook:

  • Further research is needed to clarify the intricate mechanisms of uPAR in efferocytosis.

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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
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Improved Lipofuscin Models and Quantification of Outer Segment Phagocytosis Capacity in Highly Polarized Human Retinal Pigment Epithelial Cultures
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Improved Lipofuscin Models and Quantification of Outer Segment Phagocytosis Capacity in Highly Polarized Human Retinal Pigment Epithelial Cultures

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Last Updated: Jun 21, 2026

Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells
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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

Improved Lipofuscin Models and Quantification of Outer Segment Phagocytosis Capacity in Highly Polarized Human Retinal Pigment Epithelial Cultures
10:39

Improved Lipofuscin Models and Quantification of Outer Segment Phagocytosis Capacity in Highly Polarized Human Retinal Pigment Epithelial Cultures

Published on: April 14, 2023

  • Resolving the controversies surrounding uPAR's role could reveal new therapeutic targets for inflammatory diseases.