A heterologous in-cell assay for investigating intermicrovillar adhesion complex interactions reveals a novel protrusion length-matching mechanism.

ABSTRACT: Solute transporting epithelial cells build arrays of microvilli on their apical surface to increase membrane scaffolding capacity and enhance function potential. In epithelial tissues such as the kidney and gut, microvilli are length-matched and assembled into tightly packed "brush borders," which are organized by ∼50-nm thread-like links that form between the distal tips of adjacent protrusions. Composed of protocadherins CDHR2 and CDHR5, adhesion links are stabilized at the tips by a cytoplasmic tripartite module containing the scaffolds USH1C and ANKS4B and the actin-based motor MYO7B. Because several questions about the formation and function of this "intermicrovillar adhesion complex" remain open, we devised a system that allows one to study individual binary interactions between spec

SUBMITTER: Weck ML 

PROVIDER: S-EPMC7705319 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature