English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The release of intercellular contacts in MDBK cells, initiated by the depletion of Ca2+ ions from the culture medium, results in the endocytotic uptake of membrane vesicles containing specific membrane constituents of the zonula adhaerens (ZA). During this process the junction-derived, endocytosed vesicles remain associated with the ZA plaque components, while the plaque and its attached actin filaments retract as a whole in a ring-like fashion from the plasma membrane, often accumulating, usually in fragments, in the juxtanuclear cytoplasm. Double-label immunofluorescence microscopy with antiplakoglobin and antivinculin has indicated that both plaque proteins colocalize with the hallmark membrane glycoprotein of this junction type, E-cadherin (uvomorulin). When HRP used as a fluid phase marker is applied to the culture medium, simultaneously with the Ca2+ ion-chelator EGTA, numerous HRP-positive vesicles are found in close association with the dislocated plaque material, suggesting that the HRP is contained in the vesicles formed upon EGTA-induced junction splitting. Immunoelectron microscopy with various cadherin-specific antibodies revealed vesicle-associated labeling, confirming the derivation of these plaque-associated vesicles from the ZA. As the desmosome-specific cadherin, desmoglein, is recovered in another type of junction-derived vesicle, which is characterized by its association with a desmoplakin-plaque, we conclude that the membrane domains of both kinds of junction are endocytosed during Ca2+ depletion but stay in different vesicle populations, emphasizing the selective interaction of the specific cadherins with their respective plaque and filament partners.

Endocytosis of junctional cadherins in bovine kidney epithelial (MDBK) cells cultured in low Ca2+ ion medium.