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    SLC26A5 solute carrier family 26 member 5 [ Homo sapiens (human) ]

    Gene ID: 375611, updated on 6-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Evaluation of inner ear damage by mastoid drilling with measurement of serum prestin (SLC26A5) levels.

    Evaluation of inner ear damage by mastoid drilling with measurement of serum prestin (SLC26A5) levels.
    Baskadem Yilmazer A, Tanrısever O, Alagoz MH, Yilmazer R, Goker AE, Tutar B, Uyar Y., Free PMC Article

    04/3/2024
    The pathogenic roles of the p.R130S prestin variant in DFNB61 hearing loss.

    The pathogenic roles of the p.R130S prestin variant in DFNB61 hearing loss.
    Takahashi S, Zhou Y, Cheatham MA, Homma K.,

    03/19/2024
    Functional Studies of Deafness-Associated Pendrin and Prestin Variants.

    Functional Studies of Deafness-Associated Pendrin and Prestin Variants.
    Takahashi S, Kojima T, Wasano K, Homma K., Free PMC Article

    03/14/2024
    Noise exposure levels predict blood levels of the inner ear protein prestin.

    Noise exposure levels predict blood levels of the inner ear protein prestin.
    Parker A, Parham K, Skoe E., Free PMC Article

    03/12/2022
    Molecular mechanism of prestin electromotive signal amplification.

    Molecular mechanism of prestin electromotive signal amplification.
    Ge J, Elferich J, Dehghani-Ghahnaviyeh S, Zhao Z, Meadows M, von Gersdorff H, Tajkhorshid E, Gouaux E., Free PMC Article

    01/8/2022
    Prestin and otolin-1 proteins in the hearing loss of adults chronically exposed to lead.

    Prestin and otolin-1 proteins in the hearing loss of adults chronically exposed to lead.
    Solis-Angeles S, Juárez-Pérez CA, Jiménez-Ramírez C, Cabello-López A, Aguilar-Madrid G, Del Razo LM.

    08/7/2021
    Deletion of exons 17 and 18 in prestin's STAS domain results in loss of function.

    Deletion of exons 17 and 18 in prestin's STAS domain results in loss of function.
    Takahashi S, Yamashita T, Homma K, Zhou Y, Zuo J, Zheng J, Cheatham MA., Free PMC Article

    10/24/2020
    prestin itself is the main regulator of intracellular chloride concentration via a route distinct from its transporter pathway.

    Current carried by the Slc26 family member prestin does not flow through the transporter pathway.
    Bai JP, Moeini-Naghani I, Zhong S, Li FY, Bian S, Sigworth FJ, Santos-Sacchi J, Navaratnam D., Free PMC Article

    07/20/2019
    extracellular loop of pendrin and prestin modulates their voltage-sensing property

    The extracellular loop of pendrin and prestin modulates their voltage-sensing property.
    Kuwabara MF, Wasano K, Takahashi S, Bodner J, Komori T, Uemura S, Zheng J, Shima T, Homma K., Free PMC Article

    01/19/2019
    Our study thus provides experimental evidence that supports a causal relationship between the R130S mutation in the prestin gene and hearing loss found in patients with this missense mutation.

    The R130S mutation significantly affects the function of prestin, the outer hair cell motor protein.
    Takahashi S, Cheatham MA, Zheng J, Homma K., Free PMC Article

    02/3/2018
    Prestin expression imparts susceptibility to 2-hydroxypropyl-beta-cyclodextrin-induced hearing loss.

    Susceptibility of outer hair cells to cholesterol chelator 2-hydroxypropyl-β-cyclodextrine is prestin-dependent.
    Takahashi S, Homma K, Zhou Y, Nishimura S, Duan C, Chen J, Ahmad A, Cheatham MA, Zheng J., Free PMC Article

    12/24/2016
    I hypothesize that serum assays of OHC specific protein, prestin, will allow detection and quantification of OHC damage before audiometric testing can identify presence of hearing loss.

    Prestin as a biochemical marker for early detection of acquired sensorineural hearing loss.
    Parham K.

    04/30/2016
    anion-pi interaction is the mechanism for the voltage-dependent response of prestin

    Glutamate transporter homolog-based model predicts that anion-π interaction is the mechanism for the voltage-dependent response of prestin.
    Lovas S, He DZ, Liu H, Tang J, Pecka JL, Hatfield MP, Beisel KW., Free PMC Article

    01/16/2016
    The findings suggest that CASK and the truncated prestin splice isoform contribute to confinement of prestin to the basolateral region of the plasma membrane.

    Generation of somatic electromechanical force by outer hair cells may be influenced by prestin-CASK interaction at the basal junction with the Deiter's cell.
    Cimerman J, Waldhaus J, Harasztosi C, Duncker SV, Dettling J, Heidrych P, Bress A, Gampe-Braig C, Frank G, Gummer AW, Oliver D, Knipper M, Zimmermann U.

    11/29/2014
    The effects of fast temperature jumps induced by an infrared (IR) laser in control and prestin (SLC26a5)-transfected human embryonic kidney (HEK) cells, are reproted.

    IR laser-induced perturbations of the voltage-dependent solute carrier protein SLC26a5.
    Okunade O, Santos-Sacchi J., Free PMC Article

    05/17/2014
    Calmodulin-prestin interaction may be involved in the medial olivocochlear-mediated modulation of cochlear amplification

    Functional regulation of the SLC26-family protein prestin by calcium/calmodulin.
    Keller JP, Homma K, Duan C, Zheng J, Cheatham MA, Dallos P., Free PMC Article

    03/15/2014
    COCH and SLC26A5 mRNA are expressed in specific structures and cells of the inner ear in archival human temporal bone

    RNA analysis of inner ear cells from formalin fixed paraffin embedded (FFPE) archival human temporal bone section using laser microdissection--a technical report.
    Kimura Y, Kubo S, Koda H, Shigemoto K, Sawabe M, Kitamura K.

    02/8/2014
    prestin subunits are individually functional within a given multimer

    The V499G/Y501H mutation impairs fast motor kinetics of prestin and has significance for defining functional independence of individual prestin subunits.
    Homma K, Duan C, Zheng J, Cheatham MA, Dallos P., Free PMC Article

    04/6/2013
    This result implies that in cell membranes prestin oligomerizes to a tetramer.

    Prestin in HEK cells is an obligate tetramer.
    Hallworth R, Nichols MG., Free PMC Article

    04/21/2012
    Four mutations (C124A, C192A, C260A, and C415A), all in nonconserved cysteinyl residues, significantly differed in their nonlinear capacitance properties compared with wild-type prestin.

    The roles of conserved and nonconserved cysteinyl residues in the oligomerization and function of mammalian prestin.
    Currall B, Rossino D, Jensen-Smith H, Hallworth R., Free PMC Article

    03/31/2012
    Observational study of genetic testing. (HuGE Navigator)

    Genotyping with a 198 mutation arrayed primer extension array for hereditary hearing loss: assessment of its diagnostic value for medical practice.
    Rodriguez-Paris J, Pique L, Colen T, Roberson J, Gardner P, Schrijver I., Free PMC Article

    09/15/2010
    These data reveal that the STAS (sulfate transporters and anti-sigma factor antagonist) domain starts immediately after the last transmembrane segment and lies beneath the lipid bilayer.

    Structure of the cytosolic portion of the motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters.
    Pasqualetto E, Aiello R, Gesiot L, Bonetto G, Bellanda M, Battistutta R.

    08/2/2010
    Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin

    Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.
    McGuire RM, Liu H, Pereira FA, Raphael RM., Free PMC Article

    03/1/2010
    This indicates that Met-225 in prestin somehow adjusts nonlinear capacitance and the motility of prestin-expressing cells.

    Mutation-induced reinforcement of prestin-expressing cells.
    Kumano S, Tan X, He DZ, Iida K, Murakoshi M, Wada H.

    01/21/2010
    analysis of novel DNA sequence variations in SLC26A5, encoding prestin

    DNA sequence analysis of SLC26A5, encoding prestin, in a patient-control cohort: identification of fourteen novel DNA sequence variations.
    Minor JS, Tang HY, Pereira FA, Alford RL., Free PMC Article

    01/21/2010
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