Journal
JOURNAL OF CELL SCIENCE
Volume 129, Issue 3, Pages 477-482Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.177527
Keywords
E-cadherin trafficking; Epithelial morphogenesis; Cell adhesion
Categories
Funding
- Biotechnology and Biological Sciences Research Council [BB/K00056X/1]
- Wellcome Trust [092096]
- Cancer Research UK [C6946/A14492]
- Biotechnology and Biological Sciences Research Council [BB/K00056X/1] Funding Source: researchfish
- BBSRC [BB/K00056X/1] Funding Source: UKRI
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The intracellular functions of classical cadherins are mediated through the direct binding of two catenins: beta-catenin and p120-catenin (also known as CTNND1 in vertebrates, and p120ctn in Drosophila). Whereas beta-catenin is crucial for cadherin function, the role of p120-catenin is less clear and appears to vary between organisms. We show here that p120-catenin has a conserved role in regulating the endocytosis of cadherins, but that its ancestral role might have been to promote endocytosis, followed by the acquisition of a new inhibitory role in vertebrates. In Drosophila, p120-catenin facilitates endocytosis of the dynamic E-cadherin-Bazooka subcomplex, which is followed by its recycling. The absence of p120-catenin stabilises this subcomplex at the membrane, reducing the ability of cells to exchange neighbours in embryos and expanding cell-cell contacts in imaginal discs.
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