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  1. Article ; Online: Lysosomal channels sensing forces.

    Riederer, Erika / Ren, Dejian

    Nature cell biology

    2024  Volume 26, Issue 3, Page(s) 318–320

    MeSH term(s) Lysosomes
    Language English
    Publishing date 2024-02-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-024-01347-5
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5169: Show issues Location:
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  2. Article ; Online: Distinct roles of the Na

    Riederer, Erika A / Moënne-Loccoz, Pierre / Valiyaveetil, Francis I

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 19, Page(s) e2121653119

    Abstract: Glutamate transporters carry out the concentrative uptake of glutamate by harnessing the ionic gradients present across cellular membranes. A central step in the transport mechanism is the coupled binding of Na+ and substrate. The sodium coupled Asp ... ...

    Abstract Glutamate transporters carry out the concentrative uptake of glutamate by harnessing the ionic gradients present across cellular membranes. A central step in the transport mechanism is the coupled binding of Na+ and substrate. The sodium coupled Asp transporter, GltPh is an archaeal homolog of glutamate transporters that has been extensively used to probe the transport mechanism. Previous studies have shown that hairpin-2 (HP2) functions as the extracellular gate for the aspartate binding site and plays a key role in the coupled binding of sodium and aspartate to GltPh. The binding sites for three Na+ ions (Na1-3) have been identified in GltPh, but the specific roles of the individual Na+ sites in the binding process have not been elucidated. In this study, we developed assays to probe Na+ binding to the Na1 and Na3 sites and to monitor the conformational switch in the NMDGT motif. We used these assays along with a fluorescence assay to monitor HP2 movement and EPR spectroscopy to show that Na+ binding to the Na3 site is required for the NMDGT conformational switch while Na+ binding to the Na1 site is responsible for the partial opening of HP2. Complete opening of HP2 requires the conformational switch of the NMDGT motif and therefore Na+ binding to both the Na1 and the Na3 sites. Based on our studies, we also propose an alternate pathway for the coupled binding of Na+ and Asp.
    MeSH term(s) Amino Acid Transport System X-AG/chemistry ; Binding Sites ; Glutamic Acid/metabolism ; Ions/metabolism ; Sodium/metabolism
    Chemical Substances Amino Acid Transport System X-AG ; Ions ; Glutamic Acid (3KX376GY7L) ; Sodium (9NEZ333N27)
    Language English
    Publishing date 2022-05-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2121653119
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    Zs.A 1148: Show issues Location:
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  3. Article ; Online: Lysosomal Ion Channels: What Are They Good For and Are They Druggable Targets?

    Riederer, Erika / Cang, Chunlei / Ren, Dejian

    Annual review of pharmacology and toxicology

    2022  Volume 63, Page(s) 19–41

    Abstract: Lysosomes play fundamental roles in material digestion, cellular clearance, recycling, exocytosis, wound repair, ... ...

    Abstract Lysosomes play fundamental roles in material digestion, cellular clearance, recycling, exocytosis, wound repair, Ca
    MeSH term(s) Humans ; Ion Channels/metabolism ; Signal Transduction ; Lysosomes/chemistry ; Lysosomes/metabolism ; Neurodegenerative Diseases/metabolism
    Chemical Substances Ion Channels
    Language English
    Publishing date 2022-09-23
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 196587-6
    ISSN 1545-4304 ; 0362-1642
    ISSN (online) 1545-4304
    ISSN 0362-1642
    DOI 10.1146/annurev-pharmtox-051921-013755
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  4. Article ; Online: Investigation of the allosteric coupling mechanism in a glutamate transporter homolog via unnatural amino acid mutagenesis.

    Riederer, Erika A / Valiyaveetil, Francis I

    Proceedings of the National Academy of Sciences of the United States of America

    2019  Volume 116, Issue 32, Page(s) 15939–15946

    Abstract: Glutamate transporters harness the ionic gradients across cell membranes for the concentrative uptake of glutamate. The sodium-coupled Asp symporter, ... ...

    Abstract Glutamate transporters harness the ionic gradients across cell membranes for the concentrative uptake of glutamate. The sodium-coupled Asp symporter, Glt
    MeSH term(s) Allosteric Regulation ; Amino Acid Transport System X-AG/chemistry ; Amino Acid Transport System X-AG/genetics ; Amino Acid Transport System X-AG/metabolism ; Amino Acids/genetics ; Fluorescence ; Kinetics ; Models, Molecular ; Mutagenesis/genetics ; Protein Structure, Secondary ; Sequence Homology, Amino Acid ; Sodium/metabolism
    Chemical Substances Amino Acid Transport System X-AG ; Amino Acids ; Sodium (9NEZ333N27)
    Language English
    Publishing date 2019-07-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1907852116
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    Zs.A 1148: Show issues Location:
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  5. Article ; Online: Structural basis for C-type inactivation in a Shaker family voltage-gated K

    Reddi, Ravikumar / Matulef, Kimberly / Riederer, Erika A / Whorton, Matthew R / Valiyaveetil, Francis I

    Science advances

    2022  Volume 8, Issue 16, Page(s) eabm8804

    Abstract: C-type inactivation is a process by which ion flux through a voltage-gated ... ...

    Abstract C-type inactivation is a process by which ion flux through a voltage-gated K
    Language English
    Publishing date 2022-04-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abm8804
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  6. Article: Structures of Gating Intermediates in a K+ channel

    Reddi, Ravikumar / Matulef, Kimberly / Riederer, Erika / Moenne-Loccoz, Pierre / Valiyaveetil, Francis I.

    Journal of molecular biology. 2021 Nov. 19, v. 433, no. 23

    2021  

    Abstract: Regulation of ion conduction through the pore of a K⁺ channel takes place through the coordinated action of the activation gate at the bundle crossing of the inner helices and the inactivation gate located at the selectivity filter. The mechanism of ... ...

    Abstract Regulation of ion conduction through the pore of a K⁺ channel takes place through the coordinated action of the activation gate at the bundle crossing of the inner helices and the inactivation gate located at the selectivity filter. The mechanism of allosteric coupling of these gates is of key interest. Here we report new insights into this allosteric coupling mechanism from studies on a W67F mutant of the KcsA channel. W67 is in the pore helix and is highly conserved in K⁺ channels. The KcsA W67F channel shows severely reduced inactivation and an enhanced rate of activation. We use continuous wave EPR spectroscopy to establish that the KcsA W67F channel shows an altered pH dependence of activation. Structural studies on the W67F channel provide the structures of two intermediate states: a pre- open state and a pre-inactivated state of the KcsA channel. These structures highlight key nodes in the allosteric pathway. The structure of the KcsA W67F channel with the activation gate open shows altered ion occupancy at the second ion binding site (S2) in the selectivity filter. This finding in combination with previous studies strongly support a requirement for ion occupancy at the S2 site for the channel to inactivate.
    Keywords electron paramagnetic resonance spectroscopy ; molecular biology ; mutants ; pH ; potassium channels
    Language English
    Dates of publication 2021-1119
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2021.167296
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  7. Article ; Online: Structures of Gating Intermediates in a K

    Reddi, Ravikumar / Matulef, Kimberly / Riederer, Erika / Moenne-Loccoz, Pierre / Valiyaveetil, Francis I

    Journal of molecular biology

    2021  Volume 433, Issue 23, Page(s) 167296

    Abstract: Regulation of ion conduction through the pore of a ... ...

    Abstract Regulation of ion conduction through the pore of a K
    MeSH term(s) Allosteric Regulation ; Binding Sites ; Ion Channel Gating ; Models, Molecular ; Mutation ; Potassium Channels/chemistry ; Potassium Channels/genetics ; Potassium Channels/metabolism ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship
    Chemical Substances Potassium Channels
    Language English
    Publishing date 2021-10-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2021.167296
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    Zs.A 867: Show issues Location:
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  8. Article ; Online: Functional characterization of neurotransmitter activation and modulation in a nematode model ligand-gated ion channel.

    Heusser, Stephanie A / Yoluk, Özge / Klement, Göran / Riederer, Erika A / Lindahl, Erik / Howard, Rebecca J

    Journal of neurochemistry

    2016  Volume 138, Issue 2, Page(s) 243–253

    Abstract: The superfamily of pentameric ligand-gated ion channels includes neurotransmitter receptors that mediate fast synaptic transmission in vertebrates, and are targets for drugs including alcohols, anesthetics, benzodiazepines, and anticonvulsants. However, ... ...

    Abstract The superfamily of pentameric ligand-gated ion channels includes neurotransmitter receptors that mediate fast synaptic transmission in vertebrates, and are targets for drugs including alcohols, anesthetics, benzodiazepines, and anticonvulsants. However, the mechanisms of ion channel opening, gating, and modulation in these receptors leave many open questions, despite their pharmacological importance. Subtle conformational changes in both the extracellular and transmembrane domains are likely to influence channel opening, but have been difficult to characterize given the limited structural data available for human membrane proteins. Recent crystal structures of a modified Caenorhabditis elegans glutamate-gated chloride channel (GluCl) in multiple states offer an appealing model system for structure-function studies. However, the pharmacology of the crystallographic GluCl construct is not well established. To establish the functional relevance of this system, we used two-electrode voltage-clamp electrophysiology in Xenopus oocytes to characterize activation of crystallographic and native-like GluCl constructs by L-glutamate and ivermectin. We also tested modulation by ethanol and other anesthetic agents, and used site-directed mutagenesis to explore the role of a region of Loop F which was implicated in ligand gating by molecular dynamics simulations. Our findings indicate that the crystallographic construct functionally models concentration-dependent agonism and allosteric modulation of pharmacologically relevant receptors. Specific substitutions at residue Leu174 in loop F altered direct L-glutamate activation, consistent with computational evidence for this region's role in ligand binding. These insights demonstrate conservation of activation and modulation properties in this receptor family, and establish a framework for GluCl as a model system, including new possibilities for drug discovery. In this study, we elucidate the validity of a modified glutamate-gated chloride channel (GluClcryst ) as a structurally accessible model for GABAA receptors. In contrast to native-like controls, GluClcryst exhibits classical activation by its neurotransmitter ligand L-glutamate. The modified channel is also sensitive to allosteric modulators associated with human GABAA receptors, and to site-directed mutations predicted to alter channel opening.
    MeSH term(s) Animals ; Chloride Channels/metabolism ; Female ; Glutamic Acid/metabolism ; Humans ; Ion Channel Gating ; Ligand-Gated Ion Channels/metabolism ; Mutagenesis, Site-Directed/methods ; Neurotransmitter Agents/metabolism ; Xenopus
    Chemical Substances Chloride Channels ; Ligand-Gated Ion Channels ; Neurotransmitter Agents ; glutamate-gated chloride channels ; Glutamic Acid (3KX376GY7L)
    Language English
    Publishing date 2016-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/jnc.13644
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  9. Article ; Online: A facile approach for the in vitro assembly of multimeric membrane transport proteins.

    Riederer, Erika A / Focke, Paul J / Georgieva, Elka R / Akyuz, Nurunisa / Matulef, Kimberly / Borbat, Peter P / Freed, Jack H / Blanchard, Scott C / Boudker, Olga / Valiyaveetil, Francis I

    eLife

    2018  Volume 7

    Abstract: Membrane proteins such as ion channels and transporters are frequently homomeric. The homomeric nature raises important questions regarding coupling between subunits and complicates the application of techniques such as FRET or DEER spectroscopy. These ... ...

    Abstract Membrane proteins such as ion channels and transporters are frequently homomeric. The homomeric nature raises important questions regarding coupling between subunits and complicates the application of techniques such as FRET or DEER spectroscopy. These challenges can be overcome if the subunits of a homomeric protein can be independently modified for functional or spectroscopic studies. Here, we describe a general approach for in vitro assembly that can be used for the generation of heteromeric variants of homomeric membrane proteins. We establish the approach using Glt
    MeSH term(s) Amino Acid Sequence ; Amino Acid Transport System X-AG/chemistry ; Amino Acid Transport System X-AG/genetics ; Amino Acid Transport System X-AG/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Electron Spin Resonance Spectroscopy ; Fluorescence Resonance Energy Transfer ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Models, Molecular ; Protein Conformation ; Protein Multimerization ; Pyrococcus horikoshii/genetics ; Pyrococcus horikoshii/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances Amino Acid Transport System X-AG ; Bacterial Proteins ; Membrane Transport Proteins
    Language English
    Publishing date 2018-06-11
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.36478
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