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Structure and insights into the function of a Ca2+-activated Cl− channel

Kane Dickson, Veronica, Pedi, Leanne, Long, Stephen B.·2014·Nature
DOI 10.1038/nature13913PMC PMC4454446
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  • This type of coordination is reminiscent of the phenylalanine rings of a proposed Cl--binding site in the bestrophin channel.

    “This type of coordination is reminiscent of the phenylalanine rings of a proposed Cl--binding site in the bestrophin channel21.”

    From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [21]

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Research works printed but not linked: 61

  1. Hartzell, C., Putzier, I. & Arreola, J. Calcium-activated chloride channels. Annu. Rev. Physiol. 67, 719–758 (2005) · DOI
  2. Caputo, A. et al. TMEM16A, a membrane protein associated with calcium-dependent chloride channel activity. Science 322, 590–594 (2008) · DOI
  3. Schroeder, B. C., Cheng, T., Jan, Y. N. & Jan, L. Y. Expression cloning of TMEM16A as a calcium-activated chloride channel subunit. Cell 134, 1019–1029 (2008) · DOI
  4. Yang, Y. et al. TMEM16A confers receptor-activated calcium-dependent chloride conductance. Nature 455, 1210–1215 (2008) · DOI
  5. Sun, H., Tsunenari, T., Yau, K.-W. & Nathans, J. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc. Natl Acad. Sci. USA 99, 4008–4013 (2002) · DOI
  6. Tsunenari, T., Nathans, J. & Yau, K.-W. Ca2+-activated Cl− current from human bestrophin-4 in excised membrane patches. J. Gen. Physiol. 127, 749–754 (2006) · DOI
  7. Hartzell, H. C., Qu, Z., Yu, K., Xiao, Q. & Chien, L.-T. Molecular physiology of bestrophins: multifunctional membrane proteins linked to best disease and other retinopathies. Physiol. Rev. 88, 639–672 (2008) · DOI
  8. Kunzelmann, K. et al. Role of the Ca2+ -activated Cl− channels bestrophin and anoctamin in epithelial cells. Biol. Chem. 392, 125–134 (2011) · DOI
  9. Gomez, N. M., Tamm, E. R. & Straubeta, O. Role of bestrophin-1 in store-operated calcium entry in retinal pigment epithelium. Pflugers Archiv. 465, 481–495 (2013) · DOI
  10. Tsunenari, T. et al. Structure-function analysis of the bestrophin family of anion channels. J. Biol. Chem. 278, 41114–41125 (2003) · DOI
  11. Qu, Z., Fischmeister, R. & Hartzell, C. Mouse bestrophin-2 is a bona fide Cl− channel: identification of a residue important in anion binding and conduction. J. Gen. Physiol. 123, 327–340 (2004) · DOI
  12. Chien, L.-T., Zhang, Z.-R. & Hartzell, H. C. Single Cl− channels activated by Ca2+ in Drosophila S2 cells are mediated by bestrophins. J. Gen. Physiol. 128, 247–259 (2006) · DOI
  13. Xiao, Q., Prussia, A., Yu, K., Cui, Y.-y. & Hartzell, H. C. Regulation of bestrophin Cl channels by calcium: role of the C terminus. J. Gen. Physiol. 132, 681–692 (2008) · DOI
  14. Marquardt, A. et al. Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best’s disease). Hum. Mol. Genet. 7, 1517–1525 (1998) · DOI
  15. Petrukhin, K. et al. Identification of the gene responsible for Best macular dystrophy. Nature Genet. 19, 241–247 (1998) · DOI
  16. Davidson, A. E. et al. Missense mutations in a retinal pigment epithelium protein, Bestrophin-1, cause retinitis pigmentosa. Am. J. Hum. Genet. 85, 581–592 (2009) · DOI
  17. Boon, C. J. et al. The spectrum of ocular phenotypes caused by mutations in the BEST1 gene. Prog. Retin. Eye Res. 28, 187–205 (2009) · DOI
  18. Xiao, Q., Hartzell, H. C. & Yu, K. Bestrophins and retinopathies. Pflügers Archiv. 460, 559–569 (2010) · DOI
  19. Kinnick, T. R. et al. Autosomal recessive vitelliform macular dystrophy in a large cohort of vitelliform macular dystrophy patients. Retina 31, 581–595 (2011) · DOI
  20. Wittström, E., Ponjavic, V., Bondeson, M. L. & Andreasson, S. Anterior segment abnormalities and angle-closure glaucoma in a family with a mutation in the BEST1 gene and Best vitelliform macular dystrophy. Ophthalmic Genet. 32, 217–227 (2011) · DOI
  21. Yu, K., Cui, Y. & Hartzell, H. C. The bestrophin mutation A243V, linked to adult-onset vitelliform macular dystrophy, impairs its chloride channel function. Invest. Ophthalmol. Vis. Sci. 47, 4956–4961 (2006) · DOI
  22. Yu, K., Qu, Z., Cui, Y. & Hartzell, H. C. Chloride channel activity of bestrophin mutants associated with mild or late-onset macular degeneration. Invest. Ophthal. Vis. Sci. 48, 4694–4705 (2007) · DOI
  23. Marchant, D. et al. New VMD2 gene mutations identified in patients affected by Best vitelliform macular dystrophy. J. Med. Genet. 44, e70 (2007) · DOI
  24. Milenkovic, V. M., Röhrl, E., Weber, B. H. F. & Strauss, O. Disease-associated missense mutations in bestrophin-1 affect cellular trafficking and anion conductance. J. Cell Sci. 124, 2988–2996 (2011) · DOI
  25. Bharill, S., Fu, Z., Palty, R. & Isacoff, E. Y. Stoichiometry and specific assembly of Best ion channels. Proc. Natl Acad. Sci. USA 111, 6491–6496 (2014) · DOI
  26. Qu, Z. Q., Yu, K., Cui, Y.-y., Ying, C. & Hartzell, C. Activation of bestrophin Cl− channels is regulated by C-terminal domains. J. Biol. Chem. 282, 17460–17467 (2007) · DOI
  27. Kranjc, A. et al. Regulation of bestrophins by Ca2+: a theoretical and experimental study. PLoS ONE 4, e4672 (2009) · DOI
  28. Qu, Z. & Hartzell, H. C. Bestrophin Cl− channels are highly permeable to HCO3−. Am. J. Physiol. Cell Physiol. 294, C1371–C1377 (2008) · DOI
  29. Stotz, S. C. & Clapham, D. E. Anion-sensitive fluorophore identifies the Drosophila swell-activated chloride channel in a genome-wide RNA interference screen. PLoS ONE 7, e46865 (2012) · DOI
  30. Lee, S. et al. Channel-mediated tonic GABA release from glia. Science 330, 790–796 (2010) · DOI
  31. Woo, D. H. et al. TREK-1 and Best1 channels mediate fast and slow glutamate release in astrocytes upon GPCR activation. Cell 151, 25–40 (2012) · DOI
  32. O’Driscoll, K. E., Leblanc, N., Hatton, W. J. & Britton, F. C. Functional properties of murine bestrophin 1 channel. Biochem. Biophys. Res. Commun. 384, 476–481 (2009) · DOI
  33. Qu, Z. & Hartzell, C. Determinants of anion permeation in the second transmembrane domain of the mouse bestrophin-2 chloride channel. J. Gen. Physiol. 124, 371–382 (2004) · DOI
  34. Qu, Z., Chien, L.-T., Cui, Y. & Hartzell, H. C. The anion-selective pore of the bestrophins, a family of chloride channels associated with retinal degeneration. J. Neurosci. 26, 5411–5419 (2006) · DOI
  35. Gifford, J. L., Walsh, M. P. & Vogel, H. J. Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs. Biochem. J. 405, 199–221 (2007) · DOI
  36. Yuan, P., Leonetti, M. D., Hsiung, Y. & MacKinnon, R. Open structure of the Ca2+ gating ring in the high-conductance Ca2+-activated K+ channel. Nature 481, 94–97 (2012) · DOI
  37. Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T. & MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415, 287–294 (2002) · DOI · Paper page
  38. Hibbs, R. E. & Gouaux, E. Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474, 54–60 (2011) · DOI
  39. Hille, B. Ionic Channels of Excitable Membranes 2nd edn (Sinauer Associates, 1992)
  40. Dougherty, D. A. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271, 163–168 (1996) · DOI
  41. Jackson, M. R. et al. A preference for edgewise interactions between aromatic rings and carboxylate anions: the biological relevance of anion-quadrupole interactions. J. Phys. Chem. B 111, 8242–8249 (2007) · DOI
  42. Philip, V. et al. A survey of aspartate-phenylalanine and glutamate-phenylalanine interactions in the protein data bank: searching for anion-π pairs. Biochemistry 50, 2939–2950 (2011) · DOI · Paper page
  43. Thomas, K. A., Smith, G. M., Thomas, T. B. & Feldmann, R. J. Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments. Proc. Natl Acad. Sci. USA 79, 4843–4847 (1982) · DOI
  44. Kawate, T. & Gouaux, E. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14, 673–681 (2006) · DOI
  45. Kilmartin, J. V., Wright, B. & Milstein, C. Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line. J. Cell Biol. 93, 576–582 (1982) · DOI
  46. Long, S. B., Campbell, E. B. & MacKinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897–903 (2005) · DOI
  47. Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M. & Paciorek, W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D 59, 2023–2030 (2003) · DOI
  48. Minor, W., Cymborowski, M., Otwinowski, Z. & Chruszcz, M. HKL-3000: the integration of data reduction and structure solution–from diffraction images to an initial model in minutes. Acta Crystallogr. D 62, 859–866 (2006) · DOI
  49. Cowtan, K. D. ‘dm': An automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsl. Prot. Crystallogr. 31, 34–38 (1994)
  50. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010) · DOI · Paper page
  51. Brunger, A. T. Version 1.2 of the crystallography and NMR system. Nature Protocols 2, 2728–2733 (2007) · DOI
  52. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010) · DOI · Paper page
  53. Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355–367 (2011) · DOI
  54. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12–21 (2010) · DOI · Paper page
  55. Konecny, R., Baker, N. A. & McCammon, J. A. iAPBS: a programming interface to Adaptive Poisson-Boltzmann Solver (APBS). Comp. Sci. Discov. 5, 015005 (2012) · DOI
  56. Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. & Sansom, M. S. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354–360,–376 (1996) · DOI
  57. Miller, A. N. & Long, S. B. Crystal structure of the human two-pore domain potassium channel K2P1. Science 335, 432–436 (2012) · DOI
  58. Hou, X., Pedi, L., Diver, M. M. & Long, S. B. Crystal structure of the calcium release-activated calcium channel Orai. Science 338, 1308–1313 (2012) · DOI
  59. Lee, S.-Y., Letts, J. A. & MacKinnon, R. Functional reconstitution of purified human Hv1 H+ channels. J. Mol. Biol. 387, 1055–1060 (2009) · DOI
  60. Tsien, R. & Pozzan, T. Measurement of cytosolic free Ca2+ with quin2. Methods Enzymol. 172, 230–262 (1989) · DOI
  61. Schoenmakers, T. J., Visser, G. J., Flik, G. & Theuvenet, A. P. CHELATOR: an improved method for computing metal ion concentrations in physiological solutions. Biotechniques 12, 870–874,–876–879 (1992)

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Metadata

Authors
Kane Dickson, V., Pedi, L., & Long, S. B.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2014-10-22
Volume
516
Issue
7530
Pages
213-218
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature13913
PMC
PMC4454446
Cited by
202
References
1
Language
en
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