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Structure of a CLC chloride ion channel by cryo-electron microscopy
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“A number of Cl− transporting CLCs have been structurally characterized, providing a deep mechanistic basis for understanding the fluoride riboswitch-associated CLCs (42–46).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [45]
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- Jentsch, T. J. Discovery of CLC transport proteins: cloning, structure, function and pathophysiology. J. Physiol. 593, 4091–4109 (2015) · DOI
- Maduke, M., Miller, C. & Mindell, J. A. A decade of CLC chloride channels: structure, mechanism, and many unsettled questions. Annu. Rev. Biophys. Biomol. Struct. 29, 411–438 (2000) · DOI
- Miller, C. ClC chloride channels viewed through a transporter lens. Nature 440, 484–489 (2006) · DOI
- Koch, M. C. et al. The skeletal muscle chloride channel in dominant and recessive human myotonia. Science 257, 797–800 (1992) · DOI
- Simon, D. B. et al. Mutations in the chloride channel gene, CLCNKB, cause Bartter’s syndrome type III. Nature Genet. 17, 171–178 (1997) · DOI
- Fisher, S. E. et al. Isolation and partial characterization of a chloride channel gene which is expressed in kidney and is a candidate for Dent’s disease (an X-linked hereditary nephrolithiasis). Hum. Mol. Genet. 3, 2053–2059 (1994)
- Kornak, U. et al. Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man. Cell 104, 205–215 (2001) · DOI · Paper page
- Miller, C. & White, M. M. Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl Acad. Sci. USA 81, 2772–2775 (1984) · DOI
- Jentsch, T. J., Steinmeyer, K. & Schwarz, G. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 348, 510–514 (1990) · DOI
- Accardi, A. & Miller, C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl− channels. Nature 427, 803–807 (2004) · DOI
- Scheel, O., Zdebik, A. A., Lourdel, S. & Jentsch, T. J. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436, 424–427 (2005) · DOI
- Picollo, A. & Pusch, M. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436, 420–423 (2005) · DOI
- Walden, M. et al. Uncoupling and turnover in a Cl−/H+ exchange transporter. J. Gen. Physiol. 129, 317–329 (2007) · DOI · Paper page
- Jayaram, H., Accardi, A., Wu, F., Williams, C. & Miller, C. Ion permeation through a Cl−-selective channel designed from a CLC Cl−/H+ exchanger. Proc. Natl Acad. Sci. USA 105, 11194–11199 (2008) · DOI · Paper page
- Ludewig, U., Pusch, M. & Jentsch, T. J. Two physically distinct pores in the dimeric ClC-0 chloride channel. Nature 383, 340–343 (1996) · DOI
- 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
- Dutzler, R., Campbell, E. B. & MacKinnon, R. Gating the selectivity filter in ClC chloride channels. Science 300, 108–112 (2003) · DOI · Paper page
- Feng, L., Campbell, E. B., Hsiung, Y. & MacKinnon, R. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330, 635–641 (2010) · DOI · Paper page
- Adachi, S. et al. Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle’s loop and collecting ducts of rat kidney. J. Biol. Chem. 269, 17677–17683 (1994) · DOI
- Kieferle, S., Fong, P., Bens, M., Vandewalle, A. & Jentsch, T. J. Two highly homologous members of the ClC chloride channel family in both rat and human kidney. Proc. Natl Acad. Sci. USA 91, 6943–6947 (1994) · DOI
- Denton, J. S., Pao, A. C. & Maduke, M. Novel diuretic targets. Am. J. Physiol. Renal Physiol. 305, F931–F942 (2013) · DOI
- Estévez, R. et al. Barttin is a Cl− channel β-subunit crucial for renal Cl− reabsorption and inner ear K+ secretion. Nature 414, 558–561 (2001) · DOI
- Scholl, U. et al. Barttin modulates trafficking and function of ClC-K channels. Proc. Natl Acad. Sci. USA 103, 11411–11416 (2006) · DOI
- Waldegger, S. & Jentsch, T. J. Functional and structural analysis of ClC-K chloride channels involved in renal disease. J. Biol. Chem. 275, 24527–24533 (2000) · DOI
- L’Hoste, S. et al. Characterization of the mouse ClC-K1/Barttin chloride channel. Biochim. Biophys. Acta 1828, 2399–2409 (2013) · DOI
- Fahlke, C., Yu, H. T., Beck, C. L., Rhodes, T. H. & George, A. L. Jr. Pore-forming segments in voltage-gated chloride channels. Nature 390, 529–532 (1997) · DOI
- Accardi, A. & Pusch, M. Fast and slow gating relaxations in the muscle chloride channel CLC-1. J. Gen. Physiol. 116, 433–444 (2000) · DOI
- Estévez, R., Schroeder, B. C., Accardi, A., Jentsch, T. J. & Pusch, M. Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1. Neuron 38, 47–59 (2003) · DOI
- Waldegger, S. et al. Barttin increases surface expression and changes current properties of ClC-K channels. Pflugers Arch. 444, 411–418 (2002) · DOI
- Feng, L., Campbell, E. B. & MacKinnon, R. Molecular mechanism of proton transport in CLC Cl−/H+ exchange transporters. Proc. Natl Acad. Sci. USA 109, 11699–11704 (2012) · DOI · Paper page
- Markovic, S. & Dutzler, R. The structure of the cytoplasmic domain of the chloride channel ClC-Ka reveals a conserved interaction interface. Structure 15, 715–725 (2007) · DOI
- Robertson, J. L., Kolmakova-Partensky, L. & Miller, C. Design, function and structure of a monomeric ClC transporter. Nature 468, 844–847 (2010) · DOI
- Khantwal, C. M. et al. Revealing an outward-facing open conformational state in a CLC Cl−/H+ exchange transporter. eLife 5, e11189 (2016) · DOI
- Miller, C. Open-state substructure of single chloride channels from Torpedo electroplax. Phil. Trans. R. Soc. Lond. B 299, 401–411 (1982) · DOI
- Duffield, M., Rychkov, G., Bretag, A. & Roberts, M. Involvement of helices at the dimer interface in ClC-1 common gating. J. Gen. Physiol. 121, 149–161 (2003) · DOI
- Gradogna, A., Fenollar-Ferrer, C., Forrest, L. R. & Pusch, M. Dissecting a regulatory calcium-binding site of CLC-K kidney chloride channels. J. Gen. Physiol. 140, 681–696 (2012) · DOI
- Jayaram, H., Robertson, J. L., Wu, F., Williams, C. & Miller, C. Structure of a slow CLC Cl−/H+ antiporter from a cyanobacterium. Biochemistry 50, 788–794 (2011) · DOI
- Lim, H. H., Stockbridge, R. B. & Miller, C. Fluoride-dependent interruption of the transport cycle of a CLC Cl−/H+ antiporter. Nature Chem. Biol. 9, 721–725 (2013) · DOI · Paper page
- Bell, S. P., Curran, P. K., Choi, S. & Mindell, J. A. Site-directed fluorescence studies of a prokaryotic ClC antiporter. Biochemistry 45, 6773–6782 (2006) · DOI
- Basilio, D., Noack, K., Picollo, A. & Accardi, A. Conformational changes required for H+/Cl− exchange mediated by a CLC transporter. Nature Struct. Mol. Biol . 21, 456–463 (2014) · DOI
- 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
- Jardetzky, O. Simple allosteric model for membrane pumps. Nature 211, 969–970 (1966) · DOI
- Nguitragool, W. & Miller, C. Uncoupling of a CLC Cl−/H+ exchange transporter by polyatomic anions. J. Mol. Biol. 362, 682–690 (2006) · DOI
- Accardi, A., Lobet, S., Williams, C., Miller, C. & Dutzler, R. Synergism between halide binding and proton transport in a CLC-type exchanger. J. Mol. Biol. 362, 691–699 (2006) · DOI · Paper page
- Picollo, A., Malvezzi, M., Houtman, J. C. & Accardi, A. Basis of substrate binding and conservation of selectivity in the CLC family of channels and transporters. Nature Struct. Mol. Biol . 16, 1294–1301 (2009) · DOI
- Bergsdorf, E. Y., Zdebik, A. A. & Jentsch, T. J. Residues important for nitrate/proton coupling in plant and mammalian CLC transporters. J. Biol. Chem. 284, 11184–11193 (2009) · DOI
- Zifarelli, G. & Pusch, M. Conversion of the 2 Cl−/1 H+ antiporter ClC-5 in a NO3−/H+ antiporter by a single point mutation. EMBO J. 28, 175–182 (2009) · DOI
- De Angeli, A. et al. The nitrate/proton antiporter AtCLCa mediates nitrate accumulation in plant vacuoles. Nature 442, 939–942 (2006) · DOI
- Kim, J. H. et al. High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice. PLoS One 6, e18556 (2011) · DOI
- Hofmann, C. et al. Efficient gene transfer into human hepatocytes by baculovirus vectors. Proc. Natl Acad. Sci. USA 92, 10099–10103 (1995) · DOI
- Goehring, A. et al. Screening and large-scale expression of membrane proteins in mammalian cells for structural studies. Nat. Protoc. 9, 2574–2585 (2014) · DOI
- Kirchhofer, A. et al. Modulation of protein properties in living cells using nanobodies. Nature Struct. Mol. Biol . 17, 133–138 (2010) · DOI
- Lim, H. H., Fang, Y. & Williams, C. High-efficiency screening of monoclonal antibodies for membrane protein crystallography. PLoS One 6, e24653 (2011) · DOI
- Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005) · DOI
- Grant, T. & Grigorieff, N. Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6. eLife 4, e06980 (2015) · DOI
- Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015) · DOI
- Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012) · DOI · Paper page
- Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38–46 (2007) · DOI
- Rubinstein, J. L. & Brubaker, M. A. Alignment of cryo-EM movies of individual particles by optimization of image translations. J. Struct. Biol. 192, 188–195 (2015) · DOI
- Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004) · DOI
- Cardone, G., Heymann, J. B. & Steven, A. C. One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions. J. Struct. Biol. 184, 226–236 (2013) · DOI
- Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63–65 (2014) · DOI
- Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010) · DOI · Paper page
- Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355–367 (2011) · DOI
- Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D 71, 136–153 (2015) · DOI
- Nicholls, R. A., Long, F. & Murshudov, G. N. Low-resolution refinement tools in REFMAC5. Acta Crystallogr. D 68, 404–417 (2012) · DOI
- Fernández, I. S., Bai, X. C., Murshudov, G., Scheres, S. H. & Ramakrishnan, V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 157, 823–831 (2014) · DOI
- Ho, B. K. & Gruswitz, F. HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct. Biol. 8, 49 (2008) · DOI
- Chovancova, E. et al. CAVER 3.0: a tool for the analysis of transport pathways in dynamic protein structures. PLOS Comput. Biol. 8, e1002708 (2012) · DOI
- Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037–10041 (2001) · DOI
- Lawrence, M. C. & Colman, P. M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946–950 (1993) · DOI
- Fialho, D. et al. Chloride channel myotonia: exon 8 hot-spot for dominant-negative interactions. Brain 130, 3265–3274 (2007) · DOI
- Vindas-Smith, R. et al. Identification and functional characterization of CLCN1 mutations found in nondystrophic myotonia patients. Hum. Mutat. 37, 74–83 (2016) · DOI
- Mailänder, V., Heine, R., Deymeer, F. & Lehmann-Horn, F. Novel muscle chloride channel mutations and their effects on heterozygous carriers. Am. J. Hum. Genet. 58, 317–324 (1996)
- Trip, J. et al. In tandem analysis of CLCN1 and SCN4A greatly enhances mutation detection in families with non-dystrophic myotonia. Eur. J. Hum. Genet. 16, 921–929 (2008) · DOI
- Dupré, N. et al. Clinical, electrophysiologic, and genetic study of non-dystrophic myotonia in French-Canadians. Neuromuscul. Disord. 19, 330–334 (2009) · DOI
- Lorenz, C., Meyer-Kleine, C., Steinmeyer, K., Koch, M. C. & Jentsch, T. J. Genomic organization of the human muscle chloride channel CIC-1 and analysis of novel mutations leading to Becker-type myotonia. Hum. Mol. Genet. 3, 941–946 (1994) · DOI
Cited by
Sorted by citations
Membrane exporters of fluoride ion
McIlwain, B. C., Ruprecht, M. T., & Stockbridge, R. B. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071520-112507 · Cited by 69
A large‐scale evolutionary and structural analysis of CLC channels and transporters
Mishra, A., Díaz Vázquez, G., & Robertson, J. L. (2025) · Protein Science · doi:10.1002/pro.70389 · Cited by 3
Metadata
- Authors
- Park, E., Campbell, E. B., & MacKinnon, R.
- Venue
- Nature
- Published
- 2016-12-21
- Volume
- 541
- Issue
- 7638
- Pages
- 500-505
- ISSN
- 0028-0836
- 1476-4687
- PMC
- PMC5576512
- Cited by
- 164
- References
- 0
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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