TY - JOUR
T1 - Identification of a 120 kd hair-bundle myosin located near stereociliary tips
AU - Gillespie, Peter G.
AU - Wagner, Mark C.
AU - Hudspeth, A. J.
N1 - Funding Information:
We relied upon the expert technical support of Ms. L. Henry, who assisted with the biochemical experiments, and Mr. R. Jacobs, who aided with the microscopy. We also thank Dr. B. Barylko for adrenal myosin I, Dr. M. Mooseker for anti-myosin antibodies and brush-border and PI90 myosins, Dr. T. Pollard and Mr. S. Doberstein for anti-myosin antibodies, Dr. K. Kamm for an anti-myosin II antiserum, and Dr. R. Yount for NANTP. Dr. J. P. Albanesi, Ms. S. K. H. Gillespie, and members of our laboratory group provided useful commentson the manuscript. National Institutes of Health grant DC00241 supported this research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC Section 1734 solely to indicate this fact.
PY - 1993/10
Y1 - 1993/10
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0027439124&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027439124&partnerID=8YFLogxK
U2 - 10.1016/0896-6273(93)90071-X
DO - 10.1016/0896-6273(93)90071-X
M3 - Article
C2 - 8398149
AN - SCOPUS:0027439124
SN - 0896-6273
VL - 11
SP - 581
EP - 594
JO - Neuron
JF - Neuron
IS - 4
ER -