The Organization of Actin Filaments in the Stereocilia of Cochlear Hair Cells

• Published in: The Journal of cell biology 1980-07, Vol.86 (1), p.244-259
• Main Authors: Tilney, Lewis G., Derosier, David J., Mulroy, Michael J.
• Format: Article
• Language: English
• Subjects: Actins; Actins - metabolism; Adenosine Triphosphate - metabolism; Animals; Cations, Divalent - metabolism; Cell membranes; Cells; Cytoskeleton - ultrastructure; Epithelial cells; Hair cells; Hair Cells, Auditory - ultrastructure; Light; Lizards; Microfilaments; Microscopy, Electron; Microvilli; Microvilli - ultrastructure; Papillae; Phosphates; Scattering, Radiation; Stereocilia
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.86.1.244

Within each tapering stereocilium of the cochlea of the alligator lizard is a bundle of actin filaments with >3,000 filaments near the tip and only 18-29 filaments at the base where the bundle enters into the cuticular plate; there the filaments splay out as if on the surface of a cone, forming the rootlet. Decoration of the hair cells with subfragment 1 of myosin reveals that all the filaments in the stereocilia, including those that extend into the cuticular plate forming the rootlet, have unidirectional polarity, with the arrowheads pointing towards the cell center. The rest of the cuticular plate is composed of actin filaments that show random polarity, and numerous fine, 30 Å filaments that connect the rootlet filaments to each other, to the cuticular plate, and to the membrane. A careful examination of the packing of the actin filaments in the stereocilia by thin section and by optical diffraction reveals that the filaments are packed in a paracrystalline array with the crossover points of all the actin helices in near-perfect register. In transverse sections, the actin filaments are not hexagonally packed but, rather, are arranged in scalloped rows that present a festooned profile. We demonstrated that this profile is a product of the crossbridges by examining serial sections, sections of different thicknesses, and the same stereocilium at two different cutting angles. The filament packing is not altered by fixation in different media, removal of the limiting membrane by detergent extraction, or incubation of extracted hair cells in EGTA, EDTA, and Ca++ and ATP. From our results, we conclude that the stereocilia of the ear, unlike the brush border of intestinal epithelial cells, are not designed to shorten, nor do the filaments appear to slide past one another. In fact, the stereocilium is like a large, rigid structure designed to move as a lever.