Chloride channels articles within Nature Communications

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  • Article
    | Open Access

    CLC-type channels selectively transport Cl− across biological membranes, but it is unclear how discrimination between anions is maintained. Here, authors use a combination of non-natural amino acid substitutions, electrophysiology, and molecular dynamics simulations to determine Cl− specificity within this family of ion channels.

    • Lilia Leisle
    • , Kin Lam
    •  & Alessio Accardi

  • Article
    | Open Access

    Bestrophin channels are critical for physiology of the eye. Here, authors report cryo-EM structures of human bestrophins in various states at up to 1.8 Å resolution, revealing paralog-specific features that underlie molecular mechanisms of permeation.

    • Aaron P. Owji
    • , Jiali Wang
    •  & Tingting Yang

  • Article
    | Open Access

    TMEM16A, a calcium-activated chloride channel involved in multiple cellular processes, is implicated in various diseases, but its pharmacology remains poorly understood. Here, the authors combine cryo-EM and electrophysiology to elucidate the mechanism of TMEM16A inhibition by the pore blocker 1PBC.

    • Andy K. M. Lam
    • , Sonja Rutz
    •  & Raimund Dutzler

  • Article
    | Open Access

    The anion channel SLAC1 controls stomatal closure upon phosphoactivation. Here via structural analysis and electrophysiology, the authors propose an inhibition-release model where phosphorylation causes dissociation of a cytosolic plug from the SLAC1 transmembrane domains to induce conformational change in the pore-forming helices.

    • Yawen Li
    • , Yinan Ding
    •  & Linfeng Sun

  • Article
    | Open Access

    Volume-regulated anion channels (VRACs) are heteromers of LRRC8 proteins, all containing the obligatory subunit LRRC8A. Here, the authors develop and characterize nanobodies that bind LRRC8A and allosterically modulate the function of homomeric LRRC8A and endogenous heteromeric channels, hinting at functional mechanisms present in VRACs.

    • Dawid Deneka
    • , Sonja Rutz
    •  & Raimund Dutzler

  • Article
    | Open Access

    The binding of cytoplasmic Ca2+ to the anion-selective channel TMEM16A triggers a conformational change around its binding site that is coupled to the release of a gate at the constricted neck. Here authors use cryo-EM and electrophysiology to identify three hydrophobic residues at the intracellular entrance of the neck as constituents of this gate.

    • Andy K. M. Lam
    • , Jan Rheinberger
    •  & Raimund Dutzler

  • Article
    | Open Access

    The anion channel TMEM16A is activated by intracellular Ca2+ in a highly cooperative process. Here authors combine electrophysiology and autocorrelation analysis to observe the sampling of intermediate conformations during gating.

    • Andy K. M. Lam
    •  & Raimund Dutzler

  • Article
    | Open Access

    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
    •  & Cedric Govaerts

  • Article
    | Open Access

    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
    •  & Tingting Yang

  • Article
    | Open Access

    Plants have evolved to maximize energy capture while protecting their photosynthetic machinery in response to rapid variation in light conditions. Here, the authors describe a chloroplast voltage-dependent anion channel that contributes to photoprotection by fine-tuning the ion balance across the thylakoid membrane.

    • Andrei Herdean
    • , Enrico Teardo
    •  & Björn Lundin

  • Article |

    The ClC family of chloride channels are homodimeric and contain two pores that are gated simultaneously. Bennetts and Parker combine homology modelling and mutant-cycle analysis to reveal structural linkages important for coordination of gating between subunits.

    • Brett Bennetts
    •  & Michael W. Parker

  • Article
    | Open Access

    The vomeronasal organ detects pheromones, which are thought to activate TRPC2 channels on the surface of vomeronasal neurons. Using TRPC2 knockout mice, the authors show that urinary pheromones can also activate these neurons via calcium-activated chloride channels, suggesting a TRPC2-independent pathway for sensing pheromones.

    • SangSeong Kim
    • , Limei Ma
    •  & C. Ron Yu

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