Abstract
Mutations of MYO15A are associated with deafness in humans. In the shaker 2 mouse (Myo15a sh2), a missense mutation in the motor domain of myosin XVa causes deafness and circling behavior, and is morphologically characterized by abnormally short stereocilia bundles on the apical surface of inner ear hair cells that also lack the characteristic staircase architecture. The precise architecture of the stereocilia bundle is considered essential for normal hearing in vertebrates. Abnormally short stereocilia also result from a mutation of whirlin, a scaffolding protein that contains three PDZ domains and is a protein partner of myosin XVa. In inner ear hair cells, endogenous myosin XVa and whirlin are both present at the tips of developing and mature tereocilia, overlapping with the site of actin polymerization. Transfection of GFP-whirlin into Whrnwi hair cells or GFP-myosin XVa into Myo15a sh2 hair cells reinitiates stereocilia elongation and restores the wild-type architecture to the hair bundle. This elongation process occurs when myosin XVa interacts through its C-terminal class 1 PDZ-ligand with the third PDZ domain of whirlin and delivers whirlin to the tips of stereocilia. Thus, the programmed elongation of stereocilia to a predetermined height depends on the function of myosin XVa. Stereocilia tips are also the sites of certain components of the mechanotransduction complex. Electrophysiological analysis of hair-cell mechanotransduction in Myo15a sh2 and Whrn wi mice shows that targeting and function of the mechanotransduction complex in young postnatal mice does not depend upon programmed stereocilia elongation and staircase formation of the hair bundle mediated by the myosin XVa-whirlin complex.
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Boger, E.T., Frolenkov, G.I., Friedman, T.B., Belyantseva, I.A. (2008). Myosin XVA. In: Myosins. Proteins and Cell Regulation, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6519-4_16
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