ANKS4B Is Essential for Intermicrovillar Adhesion Complex Formation

Citations of this article
Mendeley users who have this article in their library.


Transporting and sensory epithelial cells shape apical specializations using protocadherin-based adhesion. In the enterocyte brush border, protocadherin function requires a complex of cytoplasmic binding partners, although the composition of this complex and logic governing its assembly remain poorly understood. We found that ankyrin repeat and sterile α motif domain containing 4B (ANKS4B) localizes to the tips of adherent brush border microvilli and is essential for intermicrovillar adhesion. ANKS4B interacts with USH1C and MYO7B, which link protocadherins to the actin cytoskeleton. ANKS4B and USH1C also bind to the MYO7B cargo-binding tail at distinct sites. However, a tripartite complex only forms if ANKS4B and MYO7B are first activated by USH1C. This study uncovers an essential role for ANKS4B in brush border assembly, reveals a hierarchy in the molecular interactions that drive intermicrovillar adhesion, and informs our understanding of diseases caused by mutations in USH1C and ankyrin repeat proteins, such as Usher syndrome. Epithelial cells shape apical specializations using extracellular adhesion. The enterocyte brush border offers a specific example in which microvilli are organized in a protocadherin-dependent manner. Crawley et al. report that brush border assembly requires the ankyrin repeat protein ANKS4B, which plays an essential role in stabilizing protocadherin-based intermicrovillar adhesion complexes.




Crawley, S. W., Weck, M. L., Grega-Larson, N. E., Shifrin, D. A., & Tyska, M. J. (2016). ANKS4B Is Essential for Intermicrovillar Adhesion Complex Formation. Developmental Cell, 36(2), 190–200.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free