During development, Schwann cells (SCs) interpret different extracellular cues 
to regulate their migration, proliferation, and the remarkable morphological 
changes associated with the sorting, ensheathment, and myelination of axons. 
Although interactions between extracellular matrix proteins and integrins are 
critical to some of these processes, the downstream signaling pathways they 
control are still poorly understood. Integrin-linked kinase (ILK) is a focal 
adhesion protein that associates with multiple binding partners to link 
integrins to the actin cytoskeleton and is thought to participate in integrin 
and growth factor-mediated signaling. Using SC-specific gene ablation, we report 
essential functions for ILK in radial sorting of axon bundles and in 
remyelination in the peripheral nervous system. Our in vivo and in vitro 
experiments show that ILK negatively regulates Rho/Rho kinase signaling to 
promote SC process extension and to initiate radial sorting. ILK also 
facilitates axon remyelination, likely by promoting the activation of downstream 
molecules such as AKT/protein kinase B.