The remarkable lifelong stability of mechanotransducing stereocilia of the inner ear hair cells depends on the activity of the transduction ion channels located at the tips of these mechanosensory projections.

Super-resolution microscopy reveals a highly organized compartment in the stereocilia of mechanosensory hair cells of the inner ear, which is critical for hair cell function and affected in disease.

A new purification method for stereocilia membranes enables efficient immunoaffinity purification of rare protein complexes from hair cell stereocilia, including the newly described complex of deafness genes PDZD7 and MYO7A.

Direct imaging of individual molecules of the tip-link protein PCDH15 in mouse stereocilia shows that it assembles as a dimer, forms complexes that span stereocilia, and occurs in clusters with multiple copies of the PCDH15 dimer.

Two myosin 15 isoforms are required separately for the development and long-term maintenance of hearing.

A novel mechanism for F-actin repair is involved in the maintenance of sensory hair cells and hearing function.

Emx2 reverses hair bundle orientation in sensory hair cells.

Murine TOMT is essential for transport of mechanotransduction components to stereocilia in cochlear hair cells.

The tail domain of Myosin III binds to and cross-links actin bundling protein Espin1 and thus modulates higher order actin bundle structures in cellular processes such as stereocilia and microvilli.

Structures of a mouse PCDH15 and LHFPL5 complex, two proteins involved in converting sound into electrical signals, illuminate how mechanical stimuli are delivered to the membrane of inner ear hair cells.