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  1. Article ; Online: Correction: Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity.

    Linsdell, Paul

    The Journal of membrane biology

    2024  Volume 257, Issue 1-2, Page(s) 143–149

    Language English
    Publishing date 2024-01-18
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 3082-x
    ISSN 1432-1424 ; 0022-2631
    ISSN (online) 1432-1424
    ISSN 0022-2631
    DOI 10.1007/s00232-023-00304-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity.

    Linsdell, Paul

    The Journal of membrane biology

    2023  Volume 256, Issue 4-6, Page(s) 433–442

    Abstract: Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. Structural analysis of CFTR has identified a narrow, hydrophobic region close to the extracellular end of the open channel pore that ... ...

    Abstract Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. Structural analysis of CFTR has identified a narrow, hydrophobic region close to the extracellular end of the open channel pore that may function as a selectivity filter. The present study combines comprehensive mutagenesis of hydrophobic amino-acid side-chains within the selectivity filter with functional evaluation of channel Cl
    MeSH term(s) Chloride Channels ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Amino Acids/genetics ; Mutation ; Anions/metabolism
    Chemical Substances Chloride Channels ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Amino Acids ; Anions
    Language English
    Publishing date 2023-10-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3082-x
    ISSN 1432-1424 ; 0022-2631
    ISSN (online) 1432-1424
    ISSN 0022-2631
    DOI 10.1007/s00232-023-00294-w
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  3. Article ; Online: Monovalent: Divalent Anion Selectivity in the CFTR Channel Pore.

    Linsdell, Paul

    Cell biochemistry and biophysics

    2021  Volume 79, Issue 4, Page(s) 863–871

    Abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) ... ...

    Abstract The cystic fibrosis transmembrane conductance regulator (CFTR) Cl
    MeSH term(s) Cystic Fibrosis Transmembrane Conductance Regulator
    Chemical Substances Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2021-05-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1357904-6
    ISSN 1559-0283 ; 1085-9195
    ISSN (online) 1559-0283
    ISSN 1085-9195
    DOI 10.1007/s12013-021-00998-7
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  4. Article ; Online: On the relationship between anion binding and chloride conductance in the CFTR anion channel.

    Linsdell, Paul

    Biochimica et biophysica acta. Biomembranes

    2021  Volume 1863, Issue 4, Page(s) 183558

    Abstract: Mutations at many sites within the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel pore region result in changes in chloride conductance. Although chloride binding in the pore - as well as interactions between concurrently ... ...

    Abstract Mutations at many sites within the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel pore region result in changes in chloride conductance. Although chloride binding in the pore - as well as interactions between concurrently bound chloride ions - are thought to be important facets of the chloride permeation mechanism, little is known about the relationship between anion binding and chloride conductance. The present work presents a comprehensive investigation of a number of anion binding properties in different pore mutants with differential effects on chloride conductance. When multiple pore mutants are compared, conductance appears best correlated with the ability of anions to bind to the pore when it is already occupied by chloride ions. In contrast, conductance was not correlated with biophysical measures of anion:anion interactions inside the pore. Although these findings suggest anion binding is required for high conductance, mutations that strengthened anion binding had very little effect on conductance, especially at high chloride concentrations, suggesting that the wild-type CFTR pore is already close to saturated with chloride ions. These results are used to support a revised model of chloride permeation in CFTR in which the overall chloride occupancy of multiple loosely-defined chloride binding sites results in high chloride conductance through the pore.
    MeSH term(s) Amino Acid Substitution ; Chlorides/chemistry ; Chlorides/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Humans ; Ion Transport ; Mutation, Missense
    Chemical Substances CFTR protein, human ; Chlorides ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2021-01-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2021.183558
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  5. Article ; Online: Cystic fibrosis transmembrane conductance regulator (CFTR): Making an ion channel out of an active transporter structure.

    Linsdell, Paul

    Channels (Austin, Tex.)

    2018  Volume 12, Issue 1, Page(s) 284–290

    Abstract: Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is a member of the ATP-binding cassette (ABC) family of membrane transport proteins, most members of which function as ATP-dependent pumps. ... ...

    Abstract Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is a member of the ATP-binding cassette (ABC) family of membrane transport proteins, most members of which function as ATP-dependent pumps. CFTR is unique among human ABC proteins in functioning not as a pump, but as an ion channel. Recent structural data has indicated that CFTR shares broadly similar overall architecture and ATP-dependent conformational changes as other ABC proteins. Functional investigations suggest that CFTR has a unique open portal connecting the cytoplasm to the transmembrane channel pore, that allows for a continuous pathway for Cl
    MeSH term(s) Animals ; Biological Transport ; Cystic Fibrosis/genetics ; Cystic Fibrosis/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Humans
    Chemical Substances Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2018-10-24
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2262854-X
    ISSN 1933-6969 ; 1933-6950
    ISSN (online) 1933-6969
    ISSN 1933-6950
    DOI 10.1080/19336950.2018.1502585
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Molecular dynamics study of Cl

    Zeng, Zhi Wei / Linsdell, Paul / Pomès, Régis

    Cellular and molecular life sciences : CMLS

    2023  Volume 80, Issue 2, Page(s) 51

    Abstract: The recent elucidation of atomistic structures of ... ...

    Abstract The recent elucidation of atomistic structures of Cl
    MeSH term(s) Humans ; Chlorides/metabolism ; Cystic Fibrosis/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Ion Transport ; Molecular Dynamics Simulation
    Chemical Substances CFTR protein, human ; Chlorides ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2023-01-24
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-022-04621-7
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  7. Article ; Online: Architecture and functional properties of the CFTR channel pore.

    Linsdell, Paul

    Cellular and molecular life sciences : CMLS

    2017  Volume 74, Issue 1, Page(s) 67–83

    Abstract: The main function of the cystic fibrosis transmembrane conductance regulator (CFTR) is as an ion channel for the movement of small anions across epithelial cell membranes. As an ion channel, CFTR must form a continuous pathway across the cell membrane- ... ...

    Abstract The main function of the cystic fibrosis transmembrane conductance regulator (CFTR) is as an ion channel for the movement of small anions across epithelial cell membranes. As an ion channel, CFTR must form a continuous pathway across the cell membrane-referred to as the channel pore-for the rapid electrodiffusional movement of ions. This review summarizes our current understanding of the architecture of the channel pore, as defined by electrophysiological analysis and molecular modeling studies. This includes consideration of the characteristic functional properties of the pore, definition of the overall shape of the entire extent of the pore, and discussion of how the molecular structure of distinct regions of the pore might control different facets of pore function. Comparisons are drawn with closely related proteins that are not ion channels, and also with structurally unrelated proteins with anion channel function. A simple model of pore function is also described.
    MeSH term(s) Animals ; Anions/metabolism ; Cell Membrane/metabolism ; Cystic Fibrosis/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Cytoplasm/metabolism ; Humans ; Models, Molecular ; Protein Conformation
    Chemical Substances Anions ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2017-01
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-016-2389-5
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  8. Article: Structural Changes Fundamental to Gating of the Cystic Fibrosis Transmembrane Conductance Regulator Anion Channel Pore.

    Linsdell, Paul

    Advances in experimental medicine and biology

    2017  Volume 925, Page(s) 13–32

    Abstract: Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), an epithelial cell anion channel. Potentiator drugs used in the treatment of cystic fibrosis act on the channel to increase overall channel function, ...

    Abstract Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), an epithelial cell anion channel. Potentiator drugs used in the treatment of cystic fibrosis act on the channel to increase overall channel function, by increasing the stability of its open state and/or decreasing the stability of its closed state. The structure of the channel in either the open state or the closed state is not currently known. However, changes in the conformation of the protein as it transitions between these two states have been studied using functional investigation and molecular modeling techniques. This review summarizes our current understanding of the architecture of the transmembrane channel pore that controls the movement of chloride and other small anions, both in the open state and in the closed state. Evidence for different kinds of changes in the conformation of the pore as it transitions between open and closed states is described, as well as the mechanisms by which these conformational changes might be controlled to regulate normal channel gating. The ways that key conformational changes might be targeted by small compounds to influence overall CFTR activity are also discussed. Understanding the changes in pore structure that might be manipulated by such small compounds is key to the development of novel therapeutic strategies for the treatment of cystic fibrosis.
    MeSH term(s) Animals ; Chlorides/metabolism ; Cystic Fibrosis/genetics ; Cystic Fibrosis/metabolism ; Cystic Fibrosis/pathology ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Gene Expression ; Humans ; Ion Channel Gating ; Ion Transport ; Membrane Potentials/physiology ; Molecular Dynamics Simulation ; Mutation ; Protein Conformation ; Protein Stability
    Chemical Substances CFTR protein, human ; Chlorides ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2017
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 2214-8019 ; 0065-2598
    ISSN (online) 2214-8019
    ISSN 0065-2598
    DOI 10.1007/5584_2016_33
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Anion conductance selectivity mechanism of the CFTR chloride channel.

    Linsdell, Paul

    Biochimica et biophysica acta

    2016  Volume 1858, Issue 4, Page(s) 740–747

    Abstract: All ion channels are able to discriminate between substrate ions to some extent, a process that involves specific interactions between permeant anions and the so-called selectivity filter within the channel pore. In the cystic fibrosis transmembrane ... ...

    Abstract All ion channels are able to discriminate between substrate ions to some extent, a process that involves specific interactions between permeant anions and the so-called selectivity filter within the channel pore. In the cystic fibrosis transmembrane conductance regulator (CFTR) anion-selective channel, both anion relative permeability and anion relative conductance are dependent on anion free energy of hydration--anions that are relatively easily dehydrated tend to show both high permeability and low conductance. In the present work, patch clamp recording was used to investigate the relative conductance of different anions in CFTR, and the effect of mutations within the channel pore. In constitutively-active E1371Q-CFTR channels, the anion conductance sequence was Cl(-) > NO3(-) > Br(-) > formate > SCN(-) > I(-). A mutation that disrupts anion binding in the inner vestibule of the pore (K95Q) disrupted anion conductance selectivity, such that anions with different permeabilities showed almost indistinguishable conductances. Conversely, a mutation at the putative narrowest pore region that is known to disrupt anion permeability selectivity (F337A) had minimal effects on anion relative conductance. Ion competition experiments confirmed that relatively tight binding of permeant anions resulted in relatively low conductance. These results suggest that the relative affinity of ion binding in the inner vestibule of the pore controls the relative conductance of different permeant anions in CFTR, and that the pore has two physically distinct anion selectivity filters that act in series to control anion conductance selectivity and anion permeability selectivity respectively.
    MeSH term(s) Animals ; Anions/chemistry ; Anions/metabolism ; Cell Membrane Permeability ; Chloride Channels/chemistry ; Chloride Channels/metabolism ; Cricetinae ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Kidney/cytology ; Kidney/metabolism ; Mutation ; Patch-Clamp Techniques
    Chemical Substances Anions ; Chloride Channels ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2016-04
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2016.01.009
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  10. Article ; Online: Functionally additive fixed positive and negative charges in the CFTR channel pore control anion binding and conductance.

    Linsdell, Paul / Irving, Christina L / Cowley, Elizabeth A

    The Journal of biological chemistry

    2022  Volume 298, Issue 3, Page(s) 101659

    Abstract: Ion channels use charged amino-acid residues to attract oppositely charged permeant ions into the channel pore. In the cystic fibrosis transmembrane conductance regulator (CFTR) ... ...

    Abstract Ion channels use charged amino-acid residues to attract oppositely charged permeant ions into the channel pore. In the cystic fibrosis transmembrane conductance regulator (CFTR) Cl
    MeSH term(s) Anions/chemistry ; Anions/metabolism ; Arginine/chemistry ; Arginine/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Electrophysiological Phenomena ; Ion Transport ; Lysine/chemistry ; Lysine/metabolism ; Static Electricity
    Chemical Substances Anions ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Arginine (94ZLA3W45F) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2022-01-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.101659
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