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First published online October 8, 2008

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Spectrin defies convention in OHCs

Within the mammalian cochlea, outer hair cells (OHCs) amplify sounds by electromotility - the voltage- dependent contraction and elongation of the lateral plasma membrane (LPM). Electromotility is driven by the OHC transmembrane protein prestin, and the actin- and spectrin-based cortical lattice that underlies the LPM is also important in this process; however, the precise composition of the cortical lattice, and the way in which it interacts with prestin, have so far been unknown. Now, Aziz El-Amraoui and colleagues (p. 3347) characterise the composition of spectrin (which exists as an -β heterodimer) within the cortical lattice. On the basis of previous studies in red blood cells, it had been thought that the lattice included conventional spectrins - surprisingly, though, the only β-spectrin subunit that is concentrated at the cortical lattice is the unconventional βV-spectrin, which is almost twice the length of conventional β-spectrins. βV-spectrin interacts directly with other lattice components, the authors show, and its progressive postnatal recruitment to the lattice in mouse parallels that of prestin. Moreover, the pleckstrin homology domain of βV-spectrin interacts indirectly with the C-terminal cytoplasmic domain of prestin. These results shed light on the molecular basis of sound amplification in the mammalian ear.

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Related articles in JCS:

II-βV spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells

Kirian Legendre, Saaid Safieddine, Polonca Küssel-Andermann, Christine Petit, and Aziz El-Amraoui
JCS 2008 121: 3347-3356. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?