Drosophila p120-catenin is crucial for endocytosis of the dynamic E-cadherin-Bazooka complex

被引:23
作者
Bulgakova, Natalia A. [3 ,4 ]
Brown, Nicholas H. [1 ,2 ]
机构
[1] Univ Cambridge, Gurdon Inst, Tennis Court Rd, Cambridge CB2 1QN, England
[2] Univ Cambridge, Dept Physiol Dev & Neurosci, Tennis Court Rd, Cambridge CB2 1QN, England
[3] Univ Sheffield, Western Bank, Bateson Ctr, Sheffield S10 2TN, S Yorkshire, England
[4] Univ Sheffield, Western Bank, Dept Biomed Sci, Sheffield S10 2TN, S Yorkshire, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
E-cadherin trafficking; Epithelial morphogenesis; Cell adhesion; CELL-ADHESION; P120; CATENIN; POLARITY; MORPHOGENESIS; JUNCTIONS; BINDING;
D O I
10.1242/jcs.177527
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:477 / 482
页数:6
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