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  1. Article ; Online: Not so transport incompetent after all: Revisiting a CLC-7 mutant sheds new mechanistic light on lysosomal physiology.

    Accardi, Alessio

    The Journal of general physiology

    2021  Volume 153, Issue 4

    MeSH term(s) Chloride Channels ; Lysosomes
    Chemical Substances Chloride Channels
    Language English
    Publishing date 2021-02-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 3118-5
    ISSN 1540-7748 ; 0022-1295
    ISSN (online) 1540-7748
    ISSN 0022-1295
    DOI 10.1085/jgp.202012805
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  2. Article: Structural basis of closed groove scrambling by a TMEM16 protein.

    Feng, Zhang / Alvarenga, Omar E / Accardi, Alessio

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Activation of ... ...

    Abstract Activation of Ca
    Language English
    Publishing date 2024-01-30
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.11.553029
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Structural basis of closed groove scrambling by a TMEM16 protein.

    Feng, Zhang / Alvarenga, Omar E / Accardi, Alessio

    Research square

    2023  

    Abstract: Activation of ... ...

    Abstract Activation of Ca
    Language English
    Publishing date 2023-08-18
    Publishing country United States
    Document type Preprint
    DOI 10.21203/rs.3.rs-3256633/v1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: A quantitative flux assay for the study of reconstituted Cl

    Fortea, Eva / Accardi, Alessio

    Methods in enzymology

    2021  Volume 652, Page(s) 243–272

    Abstract: The recent deluge of high-resolution structural information on membrane proteins has not been accompanied by a comparable increase in our ability to functionally interrogate these proteins. Current functional assays often are not quantitative or are ... ...

    Abstract The recent deluge of high-resolution structural information on membrane proteins has not been accompanied by a comparable increase in our ability to functionally interrogate these proteins. Current functional assays often are not quantitative or are performed in conditions that significantly differ from those used in structural experiments, thus limiting the mechanistic correspondence between structural and functional experiments. A flux assay to determine quantitatively the functional properties of purified and reconstituted Cl
    MeSH term(s) Biological Transport ; Chloride Channels/metabolism ; Chlorides ; Membrane Transport Proteins ; Substrate Specificity
    Chemical Substances Chloride Channels ; Chlorides ; Membrane Transport Proteins
    Language English
    Publishing date 2021-02-27
    Publishing country United States
    Document type Journal Article
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.01.026
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  5. Article ; Online: CELL SIGNALING. Lipids link ion channels and cancer.

    Accardi, Alessio

    Science (New York, N.Y.)

    2015  Volume 349, Issue 6250, Page(s) 789–790

    MeSH term(s) Animals ; Cell Membrane/physiology ; Membrane Potentials ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phosphatidylserines/metabolism ; ras Proteins/metabolism
    Chemical Substances Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylserines ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2015-05-20
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aad0874
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  6. Article ; Online: Structure and gating of CLC channels and exchangers.

    Accardi, Alessio

    The Journal of physiology

    2015  Volume 593, Issue 18, Page(s) 4129–4138

    Abstract: Since their serendipitous discovery the CLC family of Cl(-) transporting proteins has been a never ending source of surprises. From their double-barrelled architecture to their complex structure and divergence as channels and transporters, the CLCs never ...

    Abstract Since their serendipitous discovery the CLC family of Cl(-) transporting proteins has been a never ending source of surprises. From their double-barrelled architecture to their complex structure and divergence as channels and transporters, the CLCs never cease to amaze biophysicists, biochemists and physiologists alike. These unusual functional properties allow the CLCs to fill diverse physiological niches, regulating processes that range from muscle contraction to acidification of intracellular organelles, nutrient accumulation and survival of bacteria to environmental stresses. Over the last 15 years, the availability of atomic-level information on the structure of the CLCs, coupled to the discovery that the family is divided into passive channels and secondary active transporters, has revolutionized our understanding of their function. These breakthroughs led to the identification of the key structural elements regulating gating, transport, selectivity and regulation by ligands. Unexpectedly, many lines of evidence indicate that the CLC exchangers function according to a non-conventional transport mechanism that defies the fundamental tenets of the alternating-access paradigm for exchange transport, paving the way for future unexpected insights into the principles underlying active transport and channel gating.
    MeSH term(s) Biological Transport/physiology ; Chloride Channels/metabolism ; Chlorides/metabolism ; Humans ; Ion Channel Gating/physiology ; Membrane Transport Proteins/metabolism
    Chemical Substances Chloride Channels ; Chlorides ; Membrane Transport Proteins
    Language English
    Publishing date 2015-09-15
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 3115-x
    ISSN 1469-7793 ; 0022-3751
    ISSN (online) 1469-7793
    ISSN 0022-3751
    DOI 10.1113/JP270575
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  7. Article ; Online: Reconstitution of Proteoliposomes for Phospholipid Scrambling and Nonselective Channel Assays.

    Falzone, Maria E / Accardi, Alessio

    Methods in molecular biology (Clifton, N.J.)

    2020  Volume 2127, Page(s) 207–225

    Abstract: Phospholipid scramblases catalyze the rapid trans-bilayer movement of lipids down their concentration gradients. This process is essential for numerous cellular signaling functions including cell fusion, blood coagulation, and apoptosis. The importance ... ...

    Abstract Phospholipid scramblases catalyze the rapid trans-bilayer movement of lipids down their concentration gradients. This process is essential for numerous cellular signaling functions including cell fusion, blood coagulation, and apoptosis. The importance of scramblases is highlighted by the number of human diseases caused by mutations in these proteins. Because of their indispensable function, it is essential to understand and characterize the molecular function of phospholipid scramblases. Powerful tools to measure lipid transport in cells are available. However, these approaches provide limited mechanistic insights into the molecular bases of scrambling. Here we describe in detail an in vitro phospholipid scramblase assay and the accompanying analysis which allows for determination of the macroscopic rate constants associated with phospholipid scrambling. Notably, members of the TMEM16 family of scramblases also function as nonselective ion channels. To better understand the physiological relevance of this channel function as well as its relationship to the scrambling activity of the TMEM16s we also describe in detail an in vitro flux assay to measure nonselective channel activity. Together, these two assays can be used to investigate the dual activities of the TMEM16 scramblases/nonselective channels.
    MeSH term(s) Animals ; Anoctamins/chemistry ; Anoctamins/metabolism ; Biological Assay/methods ; Fluorescence ; Humans ; Ion Channels/chemistry ; Ion Channels/metabolism ; Ion Transport ; Ions/metabolism ; Liposomes/chemistry ; Liposomes/metabolism ; Models, Theoretical ; Phospholipid Transfer Proteins/metabolism ; Phospholipids/chemistry ; Phospholipids/isolation & purification ; Phospholipids/metabolism ; Protein Renaturation ; Proteolipids/chemistry ; Proteolipids/isolation & purification ; Proteolipids/metabolism
    Chemical Substances Anoctamins ; Ion Channels ; Ions ; Liposomes ; Phospholipid Transfer Proteins ; Phospholipids ; Proteolipids ; proteoliposomes
    Language English
    Publishing date 2020-02-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-0373-4_15
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  8. Article ; Online: Unveiling the secret lives of glutamate transporters: VGLUTs engage in multiple transport modes.

    Accardi, Alessio

    Neuron

    2014  Volume 84, Issue 6, Page(s) 1110–1112

    Abstract: Accumulation of glutamate in synaptic vesicles is mediated by vesicular glutamate transporters called VGLUTs. In the current issue of Neuron, Preobraschenski et al. (2014) show that the VGLUTs, in addition to transporting glutamate, also provide the ... ...

    Abstract Accumulation of glutamate in synaptic vesicles is mediated by vesicular glutamate transporters called VGLUTs. In the current issue of Neuron, Preobraschenski et al. (2014) show that the VGLUTs, in addition to transporting glutamate, also provide the conductances necessary to maintain the appropriate voltage and pH inside these vesicles.
    MeSH term(s) Animals ; Chlorides/metabolism ; Glutamic Acid/metabolism ; Neurotransmitter Agents/metabolism ; Potassium/metabolism ; Synaptic Vesicles/metabolism ; Vesicular Glutamate Transport Protein 1/chemistry ; Vesicular Glutamate Transport Protein 1/metabolism
    Chemical Substances Chlorides ; Neurotransmitter Agents ; Vesicular Glutamate Transport Protein 1 ; Glutamic Acid (3KX376GY7L) ; Potassium (RWP5GA015D)
    Language English
    Publishing date 2014-10-07
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 808167-0
    ISSN 1097-4199 ; 0896-6273
    ISSN (online) 1097-4199
    ISSN 0896-6273
    DOI 10.1016/j.neuron.2014.12.008
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    Zs.MG 92: Show issues

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  9. Article ; Online: Author Correction: Structural basis of pH-dependent activation in a CLC transporter.

    Fortea, Eva / Lee, Sangyun / Chadda, Rahul / Argyros, Yiorgos / Sandal, Priyanka / Mahoney-Kruszka, Robyn / Ciftci, Hatice Didar / Falzone, Maria E / Huysmans, Gerard / Robertson, Janice L / Boudker, Olga / Accardi, Alessio

    Nature structural & molecular biology

    2024  Volume 31, Issue 4, Page(s) 728

    Language English
    Publishing date 2024-02-14
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-024-01242-5
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  10. Article ; Online: Structural basis of pH-dependent activation in a CLC transporter.

    Fortea, Eva / Lee, Sangyun / Chadda, Rahul / Argyros, Yiorgos / Sandal, Priyanka / Mahoney-Kruszka, Robyn / Ciftci, Hatice Didar / Falzone, Maria E / Huysmans, Gerard / Robertson, Janice L / Boudker, Olga / Accardi, Alessio

    Nature structural & molecular biology

    2024  Volume 31, Issue 4, Page(s) 644–656

    Abstract: CLCs are dimeric chloride channels and anion/proton exchangers that regulate processes such as muscle contraction and endo-lysosome acidification. Common gating controls their activity; its closure simultaneously silences both protomers, and its opening ... ...

    Abstract CLCs are dimeric chloride channels and anion/proton exchangers that regulate processes such as muscle contraction and endo-lysosome acidification. Common gating controls their activity; its closure simultaneously silences both protomers, and its opening allows them to independently transport ions. Mutations affecting common gating in human CLCs cause dominant genetic disorders. The structural rearrangements underlying common gating are unknown. Here, using single-particle cryo-electron microscopy, we show that the prototypical Escherichia coli CLC-ec1 undergoes large-scale rearrangements in activating conditions. The slow, pH-dependent remodeling of the dimer interface leads to the concerted opening of the intracellular H
    MeSH term(s) Humans ; Cryoelectron Microscopy ; Protons ; Ions/metabolism ; Chloride Channels/genetics ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Hydrogen-Ion Concentration ; Antiporters/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism
    Chemical Substances Protons ; Ions ; Chloride Channels ; CLC-ec1 protein, E coli ; Antiporters ; Escherichia coli Proteins
    Language English
    Publishing date 2024-01-26
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-023-01210-5
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