PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28422190-2 2017 Prestin"s voltage sensitivity is influenced by intracellular chloride. Chlorides 61-69 solute carrier family 26 member 5 Homo sapiens 0-7 28422190-6 2017 Prestin has been modeled, based on structural data from related anion transporters (SLC26Dg and UraA), to have a 7 + 7 inverted repeat structure with anion transport initiated by chloride binding at the intracellular cleft. Chlorides 179-187 solute carrier family 26 member 5 Homo sapiens 0-7 28422190-11 2017 We suggest that prestin itself is the main regulator of intracellular chloride concentration via a route distinct from its transporter pathway. Chlorides 70-78 solute carrier family 26 member 5 Homo sapiens 16-23 27276272-0 2016 Chloride Anions Regulate Kinetics but Not Voltage-Sensor Qmax of the Solute Carrier SLC26a5. Chlorides 0-8 solute carrier family 26 member 5 Homo sapiens 84-91 27276272-3 2016 The mechanical activity of the OHC imparted by prestin is driven by voltage and controlled by anions, chiefly intracellular chloride. Chlorides 124-132 solute carrier family 26 member 5 Homo sapiens 47-54 27276272-4 2016 Current opinion is that chloride anions control the Boltzmann characteristics of the voltage sensor responsible for prestin activity, including Qmax, the total sensor charge moved within the membrane, and Vh, a measure of prestin"s operating voltage range. Chlorides 24-32 solute carrier family 26 member 5 Homo sapiens 116-123 27276272-4 2016 Current opinion is that chloride anions control the Boltzmann characteristics of the voltage sensor responsible for prestin activity, including Qmax, the total sensor charge moved within the membrane, and Vh, a measure of prestin"s operating voltage range. Chlorides 24-32 solute carrier family 26 member 5 Homo sapiens 222-229 27276272-6 2016 Prestin"s slow transition rates and chloride-binding kinetics adversely influence these estimates, contributing to the prevalent concept that intracellular chloride level controls the quantity of sensor charge moved. Chlorides 156-164 solute carrier family 26 member 5 Homo sapiens 0-7 27276272-7 2016 By monitoring charge movement across frequency, using measures of multifrequency admittance, expanded displacement current integration, and OHC electromotility, we find that chloride influences prestin kinetics, thereby controlling charge magnitude at any particular frequency of interrogation. Chlorides 174-182 solute carrier family 26 member 5 Homo sapiens 194-201 24988347-0 2014 Chloride-driven electromechanical phase lags at acoustic frequencies are generated by SLC26a5, the outer hair cell motor protein. Chlorides 0-8 solute carrier family 26 member 5 Homo sapiens 86-93 25485080-3 2014 The model takes into account the possible chloride-bicarbonate exchange function of prestin, a protein highly expressed in the plasma membrane of OHCs. Chlorides 42-50 solute carrier family 26 member 5 Homo sapiens 84-91 24988347-4 2014 This stretched exponential behavior, which we accurately recapitulate with a new kinetic model, the meno presto model of prestin, influences the protein"s responsiveness to chloride binding and provides for delays in eM relative to membrane voltage driving force. Chlorides 173-181 solute carrier family 26 member 5 Homo sapiens 121-128 21757707-8 2011 The molecular mechanism that facilitates motor function appeared to be the same as prestin because the motor activity depended on the concentration of intracellular chloride and was blocked by salicylate treatment. Chlorides 165-173 solute carrier family 26 member 5 Homo sapiens 83-90 23431177-0 2013 Disparities in voltage-sensor charge and electromotility imply slow chloride-driven state transitions in the solute carrier SLC26a5. Chlorides 68-76 solute carrier family 26 member 5 Homo sapiens 124-131 23431177-3 2013 Here we report on simultaneous measures of prestin"s voltage-sensor charge movement (nonlinear capacitance, NLC) and eM that evidence disparities in their voltage dependence and magnitude as a function of intracellular chloride, challenging decades" old dogma that NLC reports on eM steady-state behavior. Chlorides 219-227 solute carrier family 26 member 5 Homo sapiens 43-50 17442754-7 2007 The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry. Chlorides 196-204 solute carrier family 26 member 5 Homo sapiens 114-121 20138822-7 2010 Because chloride is important for prestin function and for the efferent-mediated inhibition of cochlear output, the prestin-directed localization of CFTR to the lateral membrane of OHCs has a potential physiological significance. Chlorides 8-16 solute carrier family 26 member 5 Homo sapiens 34-41 20138822-7 2010 Because chloride is important for prestin function and for the efferent-mediated inhibition of cochlear output, the prestin-directed localization of CFTR to the lateral membrane of OHCs has a potential physiological significance. Chlorides 8-16 solute carrier family 26 member 5 Homo sapiens 116-123 19490917-6 2009 The movement of the combined charge (i.e., anion and protein charges) across the membrane is described with a Fokker-Planck equation coupled to a kinetic equation that describes the binding of chloride ions to prestin. Chlorides 193-201 solute carrier family 26 member 5 Homo sapiens 210-217 17442754-7 2007 The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry. Chlorides 66-74 solute carrier family 26 member 5 Homo sapiens 114-121 16611815-1 2006 Chloride ions have been hypothesized to interact with the membrane outer hair cell (OHC) motor protein, prestin on its intracellular domain to confer voltage sensitivity (Oliver et al., 2001). Chlorides 0-8 solute carrier family 26 member 5 Homo sapiens 104-111 16611815-5 2006 Using the well known ototoxicant, salicylate, which competes with the putative anion binding or interaction site of prestin to assess level-dependent interactions of chloride with prestin, we determined that the resting level of chloride in OHCs is near or below 10 mm, whereas perilymphatic levels are known to be approximately 140 mm. Chlorides 166-174 solute carrier family 26 member 5 Homo sapiens 180-187 16611815-5 2006 Using the well known ototoxicant, salicylate, which competes with the putative anion binding or interaction site of prestin to assess level-dependent interactions of chloride with prestin, we determined that the resting level of chloride in OHCs is near or below 10 mm, whereas perilymphatic levels are known to be approximately 140 mm. Chlorides 229-237 solute carrier family 26 member 5 Homo sapiens 116-123 16611815-5 2006 Using the well known ototoxicant, salicylate, which competes with the putative anion binding or interaction site of prestin to assess level-dependent interactions of chloride with prestin, we determined that the resting level of chloride in OHCs is near or below 10 mm, whereas perilymphatic levels are known to be approximately 140 mm. Chlorides 229-237 solute carrier family 26 member 5 Homo sapiens 180-187 17120772-6 2006 Here, we review and extend data indicating that charge movement by prestin and consequently electromotility depend on the presence of small monovalent anions such as chloride and bicarbonate at the cytoplasmic side of the membrane. Chlorides 166-174 solute carrier family 26 member 5 Homo sapiens 67-74 15596517-1 2005 The outer hair cell (OHC) underlies mammalian cochlea amplification, and its lateral membrane motor, prestin, which drives the cell"s mechanical activity, is modulated by intracellular chloride ions. Chlorides 185-193 solute carrier family 26 member 5 Homo sapiens 101-108 15596517-7 2005 Using malate as an anion replacement, we quantify chloride effects on the nonlinear charge density and operating voltage range of prestin. Chlorides 50-58 solute carrier family 26 member 5 Homo sapiens 130-137 12835843-4 2003 Substances, that compete for the chloride combining site of the motor protein prestin, such as salicylate, might have a blocking effect on the regulation of electromotility. Chlorides 33-41 solute carrier family 26 member 5 Homo sapiens 78-85 11423665-3 2001 Here, we show that voltage sensitivity is conferred to prestin by the intracellular anions chloride and bicarbonate. Chlorides 91-99 solute carrier family 26 member 5 Homo sapiens 55-62 11914517-5 2002 Nevertheless, the association of the cloned motor protein "prestin" with an anion transporter superfamily provides clues about the molecular nature of the OHC motor in the basolateral membrane, the utilisation of chloride in hair cells and the long-term stability of small basal turn cochlear hair cells. Chlorides 213-221 solute carrier family 26 member 5 Homo sapiens 59-66 11914518-8 2002 Recently, intracellular anions (chloride or bicarbonate) were found to be essential for OHC electromotility and prestin"s function. Chlorides 32-40 solute carrier family 26 member 5 Homo sapiens 112-119 35022426-7 2022 Mutation of prestin"s chloride binding site removes salicylate competition with anions while retaining the prestin characteristic displacement currents (Nonlinear Capacitance), undermining the extrinsic voltage sensor hypothesis for prestin function. Chlorides 22-30 solute carrier family 26 member 5 Homo sapiens 12-19 34390643-4 2021 Cryoelectron microscopy (cryo-EM) structures of human prestin bound with chloride or salicylate at a common "anion site" adopt contracted or expanded states, respectively. Chlorides 73-81 solute carrier family 26 member 5 Homo sapiens 54-61 11087667-3 2000 Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell. Chlorides 175-183 solute carrier family 26 member 5 Homo sapiens 244-251 11087667-3 2000 Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell. Chlorides 175-183 solute carrier family 26 member 5 Homo sapiens 253-260 34987017-10 2021 Most important, distinct conformations were observed when purifying and imaging prestin bound to either its physiological ligand, chloride, or to competitively inhibitory anions, sulfate or salicylate. Chlorides 130-138 solute carrier family 26 member 5 Homo sapiens 80-87 35022426-7 2022 Mutation of prestin"s chloride binding site removes salicylate competition with anions while retaining the prestin characteristic displacement currents (Nonlinear Capacitance), undermining the extrinsic voltage sensor hypothesis for prestin function. Chlorides 22-30 solute carrier family 26 member 5 Homo sapiens 107-114