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Sensitivity of prestin-based membrane motor to membrane thickness.
- Source :
-
Biophysical journal [Biophys J] 2010 Jun 16; Vol. 98 (12), pp. 2831-8. - Publication Year :
- 2010
-
Abstract
- Prestin is the membrane protein in outer hair cells that harnesses electrical energy by changing its membrane area in response to changes in the membrane potential. To examine the effect of membrane thickness on this protein, phosphatidylcholine (PC) with various acyl-chain lengths were incorporated into the plasma membrane by using gamma-cyclodextrin. Incorporation of short chain PCs increased the linear capacitance and positively shifted the voltage dependence of prestin, up to 120 mV, in cultured cells. PCs with long acyl chains had the opposite effects. Because the linear capacitance is inversely related to the membrane thickness, these voltage shifts are attributable to membrane thickness. The corresponding voltage shifts of electromotility were observed in outer hair cells. These results demonstrate that electromotility is extremely sensitive to the thickness of the plasma membrane, presumably involving hydrophobic mismatch. These observations indicate that the extended state of the motor molecule, which is associated with the elongation of outer hair cells, has a conformation with a shorter hydrophobic height in the lipid bilayer.<br /> ((c) 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Animals
Cell Line
Cell Movement
Electric Capacitance
Guinea Pigs
Hair Cells, Auditory, Outer cytology
Hair Cells, Auditory, Outer metabolism
Humans
Molecular Motor Proteins chemistry
Nonlinear Dynamics
Phosphatidylcholines chemistry
Phosphatidylcholines metabolism
Protein Conformation
Proteins chemistry
Transfection
gamma-Cyclodextrins chemistry
gamma-Cyclodextrins metabolism
Cell Membrane chemistry
Cell Membrane metabolism
Molecular Motor Proteins metabolism
Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1542-0086
- Volume :
- 98
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Biophysical journal
- Publication Type :
- Academic Journal
- Accession number :
- 20550895
- Full Text :
- https://doi.org/10.1016/j.bpj.2010.03.034