ArticleBiophysical journal2010
Sensitivity of prestin-based membrane motor to membrane thickness.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- From transporter to motor: Evolutionary and structural insights into the emergence of prestin's area-motor activity in mammals.Protein science : a publication of the Protein Society · 2026Article
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025Article
- Advantages and Prospective Implications of Smart Materials in Tissue Engineering: Piezoelectric, Shape Memory, and Hydrogels.Pharmaceutics · 2023Review
- Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.Nature communications · 2022Article
- Coupling between outer hair cell electromotility and prestin sensor charge depends on voltage operating point.Hearing research · 2022Article
- Single particle cryo-EM structure of the outer hair cell motor protein prestin.Nature communications · 2022Article
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- Diflunisal inhibits prestin by chloride-dependent mechanism.PloS one · 2017Article
- Susceptibility of outer hair cells to cholesterol chelator 2-hydroxypropyl-β-cyclodextrine is prestin-dependent.Scientific reports · 2016Article
- The V499G/Y501H mutation impairs fast motor kinetics of prestin and has significance for defining functional independence of individual prestin subunits.The Journal of biological chemistry · 2013Article
- Membrane cholesterol strongly influences confined diffusion of prestin.Biophysical journal · 2012Article
- The capacitance and electromechanical coupling of lipid membranes close to transitions: the effect of electrostriction.Biophysical journal · 2012Article
- Membrane thickness sensitivity of prestin orthologs: the evolution of a piezoelectric protein.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.