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    PKD2L1 polycystin 2 like 1, transient receptor potential cation channel [ Homo sapiens (human) ]

    Gene ID: 9033, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Genetic Variants in WNT16 and PKD2L1 Locus Affect Heel Ultrasound Bone Stiffness: Analyses from the General Population and Patients Evaluated for Osteoporosis.

    Genetic Variants in WNT16 and PKD2L1 Locus Affect Heel Ultrasound Bone Stiffness: Analyses from the General Population and Patients Evaluated for Osteoporosis.
    Kragl A, Hannemann A, Nauck M, Völker U, Siggelkow H, Teumer A, Tzvetkov MV., Free PMC Article

    11/2/2023
    Polycystic kidney disease 2-like 1 channel contributes to the bitter aftertaste perception of quinine.

    Polycystic kidney disease 2-like 1 channel contributes to the bitter aftertaste perception of quinine.
    Shimizu T, Fujii T, Hanita K, Shinozaki R, Takamura Y, Suzuki Y, Kageyama T, Kato M, Nishijo H, Tominaga M, Sakai H., Free PMC Article

    03/22/2023
    Molecular Mechanism of L-Pyroglutamic Acid Interaction with the Human Sour Receptor.

    Molecular Mechanism of L-Pyroglutamic Acid Interaction with the Human Sour Receptor.
    Eom S, Lee S, Lee J, Pyeon M, Yeom HD, Song JH, Choi EJ, Lee M, Lee JH, Chang JY., Free PMC Article

    03/7/2023
    Adaptive selection drives TRPP3 loss-of-function in an Ethiopian population.

    Adaptive selection drives TRPP3 loss-of-function in an Ethiopian population.
    Walsh S, Izquierdo-Serra M, Acosta S, Edo A, Lloret M, Moret R, Bosch E, Oliva B, Bertranpetit J, Fernández-Fernández JM., Free PMC Article

    01/16/2021
    Opening TRPP2 (PKD2L1) requires the transfer of gating charges.

    Opening TRPP2 (PKD2L1) requires the transfer of gating charges.
    Ng LCT, Vien TN, Yarov-Yarovoy V, DeCaen PG., Free PMC Article

    03/28/2020
    Charge-neutralizing mutations (K452Q, K455Q and K461Q) in transmembrane segment 4 reduced gating charges, positively shifted the Boltzmann-type activation curve [i.e., open probability (P open)-V curve] and altered the time-courses of activation/deactivation of PKD2L1, indicating that this region constitutes part of a voltage sensor.

    Integrative Approach with Electrophysiological and Theoretical Methods Reveals a New Role of S4 Positively Charged Residues in PKD2L1 Channel Voltage-Sensing.
    Numata T, Tsumoto K, Yamada K, Kurokawa T, Hirose S, Nomura H, Kawano M, Kurachi Y, Inoue R, Mori Y., Free PMC Article

    04/20/2019
    The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here the authors show that these differences are reflected in the architecture of polycystin 2-l1.

    Cryo-EM structure of the polycystin 2-l1 ion channel.
    Hulse RE, Li Z, Huang RK, Zhang J, Clapham DE., Free PMC Article

    03/30/2019
    Clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 are significant for the channel regulation by phosphorylation.

    Identification of clustered phosphorylation sites in PKD2L1: how PKD2L1 channel activation is regulated by cyclic adenosine monophosphate signaling pathway.
    Park EYJ, Kwak M, Ha K, So I.

    03/9/2019
    The pore helix and transmembrane segment 6 of PKD2L1 are involved in upper and lower-gate opening, adopt an open conformation.

    Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1.
    Su Q, Hu F, Liu Y, Ge X, Mei C, Yu S, Shen A, Zhou Q, Yan C, Lei J, Zhang Y, Liu X, Wang T., Free PMC Article

    12/22/2018
    PKD2 and PKD1 genes are mutated in autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2.

    Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels.
    Zheng W, Yang X, Hu R, Cai R, Hofmann L, Wang Z, Hu Q, Liu X, Bulkley D, Yu Y, Tang J, Flockerzi V, Cao Y, Cao E, Chen XZ., Free PMC Article

    12/22/2018
    palmitoylation at Cys-38 and phosphorylation at Thr-39 independently regulated TRPP3 channel function

    Regulation of TRPP3 Channel Function by N-terminal Domain Palmitoylation and Phosphorylation.
    Zheng W, Yang J, Beauchamp E, Cai R, Hussein S, Hofmann L, Li Q, Flockerzi V, Berthiaume LG, Tang J, Chen XZ., Free PMC Article

    05/27/2017
    our study identified C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggest that PKD2L1 and PKD2L1/PKD1L3 channels share the PKD2L1 trimerization process.

    A novel PKD2L1 C-terminal domain critical for trimerization and channel function.
    Zheng W, Hussein S, Yang J, Huang J, Zhang F, Hernandez-Anzaldo S, Fernandez-Patron C, Cao Y, Zeng H, Tang J, Chen XZ., Free PMC Article

    03/26/2016
    Trimerization may be important for both homo- and possibly heteromeric assemblies of PKD2L1.

    Crystal structure and characterization of coiled-coil domain of the transient receptor potential channel PKD2L1.
    Molland KL, Paul LN, Yernool DA.

    04/6/2013
    This study demonistrated that human PKD2L play the role of food preference behavior.

    Behavioral analysis of Drosophila transformants expressing human taste receptor genes in the gustatory receptor neurons.
    Adachi R, Sasaki Y, Morita H, Komai M, Shirakawa H, Goto T, Furuyama A, Isono K.

    12/8/2012
    Pkd2L1 is a novel target channel whose function is regulated by the versatile scaffolding protein RACK1.

    Receptor for activated C kinase 1 (RACK1) inhibits function of transient receptor potential (TRP)-type channel Pkd2L1 through physical interaction.
    Yang J, Wang Q, Zheng W, Tuli J, Li Q, Wu Y, Hussein S, Dai XQ, Shafiei S, Li XG, Shen PY, Tu JC, Chen XZ., Free PMC Article

    04/28/2012
    Despite the moderate sequence identity between C-terminal regulatory domains (CRDs) of PKD2 and PKD2L1, they both form trimers, implying that trimeric organization of CRDs may be true of all polycystin channels.

    Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2.
    Molland KL, Narayanan A, Burgner JW, Yernool DA.

    07/5/2010
    the PKD2L1-PKD1L3 complex is involved in acid sensing in vivo

    Activation of polycystic kidney disease-2-like 1 (PKD2L1)-PKD1L3 complex by acid in mouse taste cells.
    Kawaguchi H, Yamanaka A, Uchida K, Shibasaki K, Sokabe T, Maruyama Y, Yanagawa Y, Murakami S, Tominaga M., Free PMC Article

    06/28/2010
    Observational study of gene-disease association. (HuGE Navigator)

    A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease.
    Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, Kauwe JS, Maxwell TJ, Cherny S, Doil L, Tacey K, van Luchene R, Myers A, Wavrant-De Vrièze F, Kaleem M, Hollingworth P, Jehu L, Foy C, Archer N, Hamilton G, Holmans P, Morris CM, Catanese J, Sninsky J, White TJ, Powell J, Hardy J, O'Donovan M, Lovestone S, Jones L, Morris JC, Thal L, Owen M, Williams J, Goate A., Free PMC Article

    12/2/2009
    Taken together, alpha-actinin not only attaches TRPP3 to the cytoskeleton but also up-regulates TRPP3 channel function.

    Direct binding of alpha-actinin enhances TRPP3 channel activity.
    Li Q, Dai XQ, Shen PY, Wu Y, Long W, Chen CX, Hussain Z, Wang S, Chen XZ.

    01/21/2010
    The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation.

    The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation.
    Li Q, Liu Y, Zhao W, Chen XZ.

    01/21/2010
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