ArticleThe Journal of physiology2005
Effects of cyclic nucleotides on the function of prestin.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 79 citations in OpenAlex.
- Regulation of cochlear hair cell function by intracellular calcium stores.Frontiers in cellular neuroscience · 2024Article
- A novel theoretical framework reveals more than one voltage-sensing pathway in the lateral membrane of outer hair cells.The Journal of general physiology · 2020Article
- Prestin kinetics and corresponding frequency dependence augment during early development of the outer hair cell within the mouse organ of Corti.Scientific reports · 2019Article
- The extracellular loop of pendrin and prestin modulates their voltage-sensing property.The Journal of biological chemistry · 2018Article
- Diflunisal inhibits prestin by chloride-dependent mechanism.PloS one · 2017Article
- The potential and electric field in the cochlear outer hair cell membrane.Medical & biological engineering & computing · 2015Article
- Expression of prestin in OHCs is reduced in Spag6 gene knockout mice.Neuroscience letters · 2015Article
- Prestin at year 14: progress and prospect.Hearing research · 2014Review
- Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters.Nature communications · 2014Article
- Membrane cholesterol strongly influences confined diffusion of prestin.Biophysical journal · 2012Article
- A motif of eleven amino acids is a structural adaptation that facilitates motor capability of eutherian prestin.Journal of cell science · 2012Article
- Prestin in HEK cells is an obligate tetramer.Journal of neurophysiology · 2012Article
- The roles of conserved and nonconserved cysteinyl residues in the oligomerization and function of mammalian prestin.Journal of neurophysiology · 2011Article
- Dissecting the electromechanical coupling mechanism of the motor-protein prestin.Communicative & integrative biology · 2011Article
- Selective cell-surface labeling of the molecular motor protein prestin.Biochemical and biophysical research communications · 2011Article
- Membrane thickness sensitivity of prestin orthologs: the evolution of a piezoelectric protein.Biophysical journal · 2011Article
- Prestin and the cholinergic receptor of hair cells: positively-selected proteins in mammals.Hearing research · 2011Review
- From zebrafish to mammal: functional evolution of prestin, the motor protein of cochlear outer hair cells.Journal of neurophysiology · 2011Article
- Combinatorial cysteine mutagenesis reveals a critical intramonomer role for cysteines in prestin voltage sensing.Biophysical journal · 2010Article
- Sensitivity of prestin-based membrane motor to membrane thickness.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Outer hair cells (OHCs) in the mammalian organ of Corti display electromotility, which is thought to provide the local active mechanical amplification of the cochlear response. Prestin is the key molecule responsible for OHC electromotility. Several compounds, including cGMP, have been shown to influence OHC electromotility. There are two potential cAMP/cGMP-dependent protein kinase phosphorylation sites on prestin. Whether these sites are involved in cGMP-dependent reactions is as yet unknown. In this study, prestin cDNA was transiently transfected into TSA 201 cells. Cells that expressed prestin were selected to measure non-linear capacitance (NLC), a signature of outer hair cell motility. We applied cGMP and cAMP analogues and a protein kinase G (PKG) antagonist to the cells. Furthermore, nine mutations at putative phosphorylation sites of prestin were produced. The neutral amino acid alanine replaced serine/threonine at phosphorylation sites to change the conserved phosphorylation motif in order to mimic the dephosphorylated state of prestin, whereas replacement with the negatively charged aspartic acid mimicked the phosphorylated state. The properties of such modified prestin-expressing cells were examined, through measurement of NLC and with confocal microscopy. Our data demonstrate that cGMP is significantly more influential than cAMP in modifying the non-linear, voltage-dependent charge displacement in prestin-transfected cells. The electrical properties of the single and double mutations further indicate a possible interaction between the two PKG target sites. One of these sites may influence the membrane targeting process of prestin. Finally, a new topology map of prestin is proposed.
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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.