Chloride channels

Chloride channels are ion channels activated by various triggers, including voltage, calcium and pH. Chloride channels allow passage across the membrane of chloride (Cl−) and other anions such as HCO3−, I− and NO3−. Chloride channels are important for setting a cell’s membrane potential and pH, and play a role in maintaining proper cell volume, among other functions.

Latest Research and Reviews

  • Research | | open

    The leading cause of cystic fibrosis is the deletion of phenylalanine 508 (F508del) in the first nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR). Here authors we develop nanobodies targeting NBD1 of human CFTR and demonstrate their ability to stabilize both isolated NBD1 and full-length protein.

    • Maud Sigoillot
    • , Marie Overtus
    • , Magdalena Grodecka
    • , Daniel Scholl
    • , Abel Garcia-Pino
    • , Toon Laeremans
    • , Lihua He
    • , Els Pardon
    • , Ellen Hildebrandt
    • , Ina Urbatsch
    • , Jan Steyaert
    • , John R. Riordan
    •  & Cedric Govaerts
  • Research |

    Cryo-EM analyses of human LRRC8A show a homohexameric assembly that can adopt two conformations, compact or relaxed, indicating rigid-body motions that might be involved in channel gating.

    • Go Kasuya
    • , Takanori Nakane
    • , Takeshi Yokoyama
    • , Yanyan Jia
    • , Masato Inoue
    • , Kengo Watanabe
    • , Ryoki Nakamura
    • , Tomohiro Nishizawa
    • , Tsukasa Kusakizako
    • , Akihisa Tsutsumi
    • , Haruaki Yanagisawa
    • , Naoshi Dohmae
    • , Motoyuki Hattori
    • , Hidenori Ichijo
    • , Zhiqiang Yan
    • , Masahide Kikkawa
    • , Mikako Shirouzu
    • , Ryuichiro Ishitani
    •  & Osamu Nureki
  • Research | | open

    Human Bestrophin1 (hBest1), a calcium-activated chloride channel in retinal pigment epithelium (RPE), is essential for retina physiology. Using electrophysiological and structural approaches, the authors uncover an ATP-dependent activation mechanism of hBest1, and identify an ATP-binding motif.

    • Yu Zhang
    • , Alec Kittredge
    • , Nancy Ward
    • , Changyi Ji
    • , Shoudeng Chen
    •  & Tingting Yang
  • Research |

    The structure of a homomeric channel of subunit A of leucine-rich repeat-containing protein 8 (LRRC8) determined by cryo-electron microscopy and X-ray crystallography reveals the basis for anion selectivity.

    • Dawid Deneka
    • , Marta Sawicka
    • , Andy K. M. Lam
    • , Cristina Paulino
    •  & Raimund Dutzler
    Nature 558, 254-259

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