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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
Published on: October 17, 2014
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Late domain dependent E-cadherin recruitment into extracellular vesicles
Sebastian Bänfer1, Sophie Kutscher1, Fenja Fleck1
1Department of Cell Biology and Cell Pathology, Philipps University Marburg, Marburg, Germany.
Frontiers in Cell and Developmental Biology
|September 29, 2022
Summary
E-cadherin is recruited into extracellular vesicles (EVs) via a mechanism involving the ESCRT-I component Tsg101 and a specific motif in E-cadherin. This process is crucial for exosomal E-cadherin secretion.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- E-cadherin mediates epithelial cell-cell adhesion and signaling.
- E-cadherin is detected in exosomal fractions from human body fluids.
- The mechanism for E-cadherin recruitment into extracellular vesicles (EVs) remains undefined.
Purpose of the Study:
- To elucidate the cellular mechanism of E-cadherin incorporation into EVs.
- To identify the molecular components involved in E-cadherin exosomal secretion.
Main Methods:
- Analysis of exosomal fractions.
- Investigating the role of Tsg101 and the P(S/T)AP late domain motif.
- Mutational analysis of the E-cadherin cytoplasmic tail.
Main Results:
- E-cadherin is incorporated into the EV membrane with its extracellular domain exposed.
- Recruitment depends on the ESCRT-I component Tsg101.
- A conserved P(S/T)AP late domain motif in E-cadherin mediates Tsg101 interaction.
- Mutation of the P(S/T)AP motif significantly reduces exosomal E-cadherin secretion.
Conclusions:
- The P(S/T)AP late domain-mediated exosomal recruitment process is utilized by endogenous E-cadherin.
- This mechanism highlights a novel pathway for transmembrane protein sorting into EVs.
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