4.7 Article

Late domain dependent E-cadherin recruitment into extracellular vesicles

Journal

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2022.878620

Keywords

E-cadherin; exosomes; late domain; ESCRT (endosomal sorting complex required for transport); multivesicular bodies (MVB); extracellular vesicles

Funding

  1. Deutsche Forschungsgemeinschaft (DFG), Bonn, Germany
  2. Deutsche Forschungsgemeinschaft grant [GRK 2213]
  3. [GRK2573]

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In this study, we demonstrate that E-cadherin can be recruited into the membrane of extracellular vesicles through a specific domain in its cytoplasmic tail that interacts with Tsg101. This finding contributes to a better understanding of the formation and function of 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 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.

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