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Related Concept Videos

Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Receptor-Mediated Endocytosis01:20

Receptor-Mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
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One well-characterized example of receptor-mediated endocytosis is the...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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GPCR Desensitization

G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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Related Experiment Video

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A High-content Assay for Monitoring AMPA Receptor Trafficking
10:34

A High-content Assay for Monitoring AMPA Receptor Trafficking

Published on: January 28, 2019

Endogenous cAbl regulates receptor endocytosis.

Michele Jacob1, Leslie A Todd, R Sonali Majumdar

  • 1The Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania 19104-4268, USA. mjacob@wistar.org

Cellular Signalling
|April 7, 2009
PubMed
Summary

Non-transforming cAbl kinase promotes B lymphocyte antigen receptor endocytosis by linking cytoskeletal remodeling and ubiquitylation. Abl kinase activity is essential for CrkII phosphorylation, Rac activation, and receptor internalization.

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy
10:24

Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy

Published on: April 9, 2017

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Ligand-induced receptor endocytosis involves receptor ubiquitylation and actin cytoskeleton remodeling.
  • Tyrosine kinases are crucial for both receptor endocytosis and actin reorganization.
  • Abl family kinases are unique in possessing an actin-binding domain, suggesting direct actin regulation.

Purpose of the Study:

  • To investigate the role of non-transforming cAbl kinase in ligand-induced antigen receptor endocytosis in B lymphocytes.
  • To elucidate the signaling pathways downstream of cAbl involved in receptor internalization.

Main Methods:

  • Pharmacologic inhibition and genetic deletion of cAbl in B lymphocytes.
  • Analysis of tyrosine phosphorylation of CrkII and cCbl.
  • Assessment of Rac activation.
  • Monitoring of antigen receptor capping and endocytosis.

Main Results:

  • Pharmacologic inhibition or genetic deletion of cAbl impaired tyrosine phosphorylation of CrkII.
  • cAbl inhibition or ablation led to defective Rac activation downstream of CrkII.
  • These defects resulted in impaired antigen receptor capping and endocytosis.
  • CrkII phosphorylation was essential for Rac activation, while CrkII-cCbl association and cCbl phosphorylation were cAbl-independent.

Conclusions:

  • Non-transforming cAbl kinase plays a critical role in promoting ligand-induced antigen receptor endocytosis in B lymphocytes.
  • CrkII acts as a crucial linker, connecting receptor engagement to cytoskeletal remodeling by integrating cAbl and cCbl signaling pathways.
  • This integration of signaling pathways cooperatively regulates receptor endocytosis.