Identification of a 120 kd hair-bundle myosin located near stereociliary tips

Peter G. Gillespie, Mark C. Wagner, A. J. Hudspeth

Research output: Contribution to journalArticlepeer-review

128 Scopus citations

Abstract

By adapting to sustained stimuli, hair cells of the internal ear maintain their optimal sensitivity to minute displacements. Biophysical experiments have suggested that adaptation is mediated by a molecular motor, most likely a member of the myosin family. To provide direct evidence for the presence of myosin isozymes in hair bundles, we used photoaffinity labeling with vanadate-trapped uridine and adenine nucleotides to identify proteins of 120, 160, and 230 kd in a preparation of hair bundles purified from the bullfrog's sacculus. The photoaffinity labeling properties of these proteins, particularly the 120 kd protein, resembled those of other well-characterized myosins. A 120 kd hair-bundle protein was also recognized by a monoclonal antibody directed against a vertebrate myosin I isozyme. Immunofluorescence microscopy localized this protein near the beveled top edge of the hair bundle, the site of mechano-electrical transduction and adaptation.

Original languageEnglish (US)
Pages (from-to)581-594
Number of pages14
JournalNeuron
Volume11
Issue number4
DOIs
StatePublished - Oct 1993

ASJC Scopus subject areas

  • Neuroscience(all)

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