Ankyrin-B – through interactions with PI3P lipids, dynactin and RabGAP1L – functions as a critical node in the protein circuitry underlying polarized recycling of α5β1-integrin to enable haptotaxis along fibronectin gradients.
The 24 ankyrin repeats of ankyrin proteins form an extended solenoid that provides an extremely conserved groove for binding to numerous targets via combinatorial usage of multiple weak interaction sites.
The 24 ANK repeats of each ankyrin are inhibited by combinatorial bindings of multiple disordered segments from their tail regions, suggesting a mechanism for differential regulations of membrane target bindings by ankyrins.
Analysis of AnkyrinR conditional knockout mice shows that AnkyrinR regulates PV+ fast-spiking interneurons by organizing and maintaining perineuronal nets and through the membrane clustering of Kv3.1b K+ channels.
The functional interaction of Na+ and KATP channels at the intercalated disk of cardiomyocytes depends on Ankyrin G and is clinically relevant since KATP channel mutations affect Na+ channel expression.
Super-resolution imaging reveals how the skeleton that supports the outer membrane of axons is assembled during development, and provides an explanation for why this structure preferentially forms in axons but rarely in dendrites.