Late domain dependent E-cadherin recruitment into extracellular vesicles
E-cadherin, a transmembrane protein involved in epithelial cell-cell adhesion and signaling, is found in exosomal fractions isolated from human body fluids. A cellular mechanism for recruitment of E-cadherin into extracellular vesicles (EVs) has not yet been defined. Here, we show that E-cadherin is...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-09-01
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| Series: | Frontiers in Cell and Developmental Biology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2022.878620/full |
| _version_ | 1811273371231453184 |
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| author | Sebastian Bänfer Sophie Kutscher Fenja Fleck Martina Dienst Christian Preußer Elke Pogge von Strandmann Ralf Jacob |
| author_facet | Sebastian Bänfer Sophie Kutscher Fenja Fleck Martina Dienst Christian Preußer Elke Pogge von Strandmann Ralf Jacob |
| author_sort | Sebastian Bänfer |
| collection | DOAJ |
| description | E-cadherin, a transmembrane protein involved in epithelial cell-cell adhesion and signaling, is found in exosomal fractions isolated from human body fluids. A cellular mechanism for recruitment of E-cadherin into extracellular vesicles (EVs) has not yet been defined. Here, we show that E-cadherin is incorporated into the membrane of EVs with the extracellular domain exposed at the vesicle surface. This recruitment depends on the endosomal sorting complex required for transport I (ESCRT-I) component Tsg101 and a highly conserved tetrapeptide P(S/T)AP late domain motif in the cytoplasmic tail of E-cadherin that mediates interaction with Tsg101. Mutation of this motif results in a loss of interaction and a dramatic decrease in exosomal E-cadherin secretion. We conclude, that the process of late domain mediated exosomal recruitment is exerted by this endogenous non-ESCRT transmembrane protein. |
| first_indexed | 2024-04-12T22:59:21Z |
| format | Article |
| id | doaj.art-8861f301e46140c79789ebe823b1c364 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-04-12T22:59:21Z |
| publishDate | 2022-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-8861f301e46140c79789ebe823b1c3642022-12-22T03:13:07ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2022-09-011010.3389/fcell.2022.878620878620Late domain dependent E-cadherin recruitment into extracellular vesiclesSebastian Bänfer0Sophie Kutscher1Fenja Fleck2Martina Dienst3Christian Preußer4Elke Pogge von Strandmann5Ralf Jacob6Department of Cell Biology and Cell Pathology, Philipps University Marburg, Marburg, GermanyDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, Marburg, GermanyDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, Marburg, GermanyDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, Marburg, GermanyCenter for Tumor Biology and Immunology (ZTI), Institute for Tumor Immunology, Philipps University Marburg, Marburg, GermanyCenter for Tumor Biology and Immunology (ZTI), Institute for Tumor Immunology, Philipps University Marburg, Marburg, GermanyDepartment of Cell Biology and Cell Pathology, Philipps University Marburg, Marburg, GermanyE-cadherin, a transmembrane protein involved in epithelial cell-cell adhesion and signaling, is found in exosomal fractions isolated from human body fluids. A cellular mechanism for recruitment of E-cadherin into extracellular vesicles (EVs) has not yet been defined. Here, we show that E-cadherin is incorporated into the membrane of EVs with the extracellular domain exposed at the vesicle surface. This recruitment depends on the endosomal sorting complex required for transport I (ESCRT-I) component Tsg101 and a highly conserved tetrapeptide P(S/T)AP late domain motif in the cytoplasmic tail of E-cadherin that mediates interaction with Tsg101. Mutation of this motif results in a loss of interaction and a dramatic decrease in exosomal E-cadherin secretion. We conclude, that the process of late domain mediated exosomal recruitment is exerted by this endogenous non-ESCRT transmembrane protein.https://www.frontiersin.org/articles/10.3389/fcell.2022.878620/fullE-cadherinexosomeslate domainESCRT (endosomal sorting complex required for transport)multivesicular bodies (MVB)extracellular vesicles |
| spellingShingle | Sebastian Bänfer Sophie Kutscher Fenja Fleck Martina Dienst Christian Preußer Elke Pogge von Strandmann Ralf Jacob Late domain dependent E-cadherin recruitment into extracellular vesicles Frontiers in Cell and Developmental Biology E-cadherin exosomes late domain ESCRT (endosomal sorting complex required for transport) multivesicular bodies (MVB) extracellular vesicles |
| title | Late domain dependent E-cadherin recruitment into extracellular vesicles |
| title_full | Late domain dependent E-cadherin recruitment into extracellular vesicles |
| title_fullStr | Late domain dependent E-cadherin recruitment into extracellular vesicles |
| title_full_unstemmed | Late domain dependent E-cadherin recruitment into extracellular vesicles |
| title_short | Late domain dependent E-cadherin recruitment into extracellular vesicles |
| title_sort | late domain dependent e cadherin recruitment into extracellular vesicles |
| topic | E-cadherin exosomes late domain ESCRT (endosomal sorting complex required for transport) multivesicular bodies (MVB) extracellular vesicles |
| url | https://www.frontiersin.org/articles/10.3389/fcell.2022.878620/full |
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