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  1. Article ; Online: Understanding the Molecular Regulation of Serotonin Receptor 5-HTR

    Dutta Gupta, Oindrilla / Karbat, Izhar / Pal, Kuntal

    Journal of molecular neuroscience : MN

    2023  Volume 73, Issue 7-8, Page(s) 664–677

    Abstract: The serotonin receptor subtype 5- ... ...

    Abstract The serotonin receptor subtype 5-HTR
    MeSH term(s) Humans ; Animals ; beta-Arrestin 1/metabolism ; Signal Transduction ; Phosphorylation ; Receptors, Serotonin/metabolism ; Anxiety Disorders ; beta-Arrestin 2/metabolism ; beta-Arrestin 2/pharmacology ; beta-Arrestins/metabolism ; Mammals
    Chemical Substances beta-Arrestin 1 ; Receptors, Serotonin ; beta-Arrestin 2 ; beta-Arrestins
    Language English
    Publishing date 2023-08-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1043392-2
    ISSN 1559-1166 ; 0895-8696
    ISSN (online) 1559-1166
    ISSN 0895-8696
    DOI 10.1007/s12031-023-02146-7
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    Zs.A 3006: Show issues Location:
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  2. Article ; Online: Ion channel auxiliary subunit: does one size fit all?

    Karbat, Izhar / Reuveny, Eitan

    Cell

    2021  Volume 184, Issue 2, Page(s) 299–301

    Abstract: Ion channels can tailor their activity to the particular cellular context by incorporating auxiliary subunits that are channel-type specific. In this issue of Cell, Ávalos Prado et al. now find that a well-characterized voltage-gated ... ...

    Abstract Ion channels can tailor their activity to the particular cellular context by incorporating auxiliary subunits that are channel-type specific. In this issue of Cell, Ávalos Prado et al. now find that a well-characterized voltage-gated K
    MeSH term(s) Humans ; Ion Channels
    Chemical Substances Ion Channels
    Language English
    Publishing date 2021-01-22
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.12.038
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    Zs.A 1167: Show issues Location:
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  3. Article ; Online: One-shot design elevates functional expression levels of a voltage-gated potassium channel.

    Weinstein, Jonathan Jacob / Saikia, Chandamita / Karbat, Izhar / Goldenzweig, Adi / Reuveny, Eitan / Fleishman, Sarel Jacob

    Protein science : a publication of the Protein Society

    2024  Volume 33, Issue 6, Page(s) e4995

    Abstract: Membrane proteins play critical physiological roles as receptors, channels, pumps, and transporters. Despite their importance, however, low expression levels often hamper the experimental characterization of membrane proteins. We present an automated and ...

    Abstract Membrane proteins play critical physiological roles as receptors, channels, pumps, and transporters. Despite their importance, however, low expression levels often hamper the experimental characterization of membrane proteins. We present an automated and web-accessible design algorithm called mPROSS (https://mPROSS.weizmann.ac.il), which uses phylogenetic analysis and an atomistic potential, including an empirical lipophilicity scale, to improve native-state energy. As a stringent test, we apply mPROSS to the Kv1.2-Kv2.1 paddle chimera voltage-gated potassium channel. Four designs, encoding 9-26 mutations relative to the parental channel, were functional and maintained potassium-selective permeation and voltage dependence in Xenopus oocytes with up to 14-fold increase in whole-cell current densities. Additionally, single-channel recordings reveal no significant change in the channel-opening probability nor in unitary conductance, indicating that functional expression levels increase without impacting the activity profile of individual channels. Our results suggest that the expression levels of other dynamic channels and receptors may be enhanced through one-shot design calculations.
    MeSH term(s) Animals ; Xenopus laevis ; Algorithms ; Kv1.2 Potassium Channel/genetics ; Kv1.2 Potassium Channel/metabolism ; Kv1.2 Potassium Channel/chemistry ; Oocytes/metabolism ; Phylogeny ; Shab Potassium Channels/metabolism ; Shab Potassium Channels/genetics ; Shab Potassium Channels/chemistry ; Mutation ; Xenopus
    Language English
    Publishing date 2024-05-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.4995
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  4. Article ; Online: Voltage Sensing Comes to Rest.

    Karbat, Izhar / Reuveny, Eitan

    Cell

    2019  Volume 178, Issue 4, Page(s) 776–778

    Abstract: Voltage sensing by ion channels is the key event enabling the generation and propagation of electrical activity in excitable cells. In this issue of Cell, Wisedchaisri et al. provide a structural view of a voltage-gated sodium channel in its resting ... ...

    Abstract Voltage sensing by ion channels is the key event enabling the generation and propagation of electrical activity in excitable cells. In this issue of Cell, Wisedchaisri et al. provide a structural view of a voltage-gated sodium channel in its resting closed conformation.
    MeSH term(s) Ion Channels ; Molecular Conformation ; Sodium ; Voltage-Gated Sodium Channels
    Chemical Substances Ion Channels ; Voltage-Gated Sodium Channels ; Sodium (9NEZ333N27)
    Language English
    Publishing date 2019-08-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2019.07.013
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  5. Article: Voltage Sensing Comes to Rest

    Karbat, Izhar / Reuveny, Eitan

    Elsevier Inc. Cell. 2019 Aug. 08, v. 178, no. 4

    2019  

    Abstract: Voltage sensing by ion channels is the key event enabling the generation and propagation of electrical activity in excitable cells. In this issue of Cell, Wisedchaisri et al. provide a structural view of a voltage-gated sodium channel in its resting ... ...

    Abstract Voltage sensing by ion channels is the key event enabling the generation and propagation of electrical activity in excitable cells. In this issue of Cell, Wisedchaisri et al. provide a structural view of a voltage-gated sodium channel in its resting closed conformation.
    Keywords action potentials ; cells ; electric potential difference ; ion transport ; sodium channels
    Language English
    Dates of publication 2019-0808
    Size p. 776-778.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2019.07.013
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  6. Article ; Online: Production of recombinant venom peptides as tools for ion channel research.

    Saikia, Chandamita / Ben-Nissan, Gili / Reuveny, Eitan / Karbat, Izhar

    Methods in enzymology

    2021  Volume 654, Page(s) 169–201

    Abstract: Animal venom is a rich source for peptide toxins that bind and modulate the function of ion channels. Owing to their ability to bind receptor sites on the channel protein with high affinity and specificity, peptide neurotoxins have become an ... ...

    Abstract Animal venom is a rich source for peptide toxins that bind and modulate the function of ion channels. Owing to their ability to bind receptor sites on the channel protein with high affinity and specificity, peptide neurotoxins have become an indispensable tool for ion channel research. Recent breakthroughs in structural biology and advances in computer simulations of biomolecules have sparked a new interest in animal toxins as probes of channel protein structure and function. Here, we focus on methods used to produce animal toxins for research purposes using recombinant expression. The specific challenges associated with heterologous production of venom peptides are discussed, and several methods targeting these issues are presented with an emphasis on E. coli based systems. An efficient protocol for the bacterial expression, folding, and purification of recombinant venom peptides is described.
    MeSH term(s) Animals ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Ion Channels/genetics ; Peptides ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Venoms
    Chemical Substances Ion Channels ; Peptides ; Recombinant Proteins ; Venoms
    Language English
    Publishing date 2021-03-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.01.029
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  7. Article ; Online: Store-operated Ca

    Gataulin, Diana / Kuperman, Yael / Tsoory, Michael / Biton, Inbal E / Nataniel, Tomer / Palty, Raz / Karbat, Izhar / Meshcheriakova, Anna / Reuveny, Eitan

    PNAS nexus

    2023  Volume 2, Issue 3, Page(s) pgad068

    Abstract: Store-operated calcium entry (SOCE) is a vital process aimed at refilling cellular internal ... ...

    Abstract Store-operated calcium entry (SOCE) is a vital process aimed at refilling cellular internal Ca
    Language English
    Publishing date 2023-03-04
    Publishing country England
    Document type Journal Article
    ISSN 2752-6542
    ISSN (online) 2752-6542
    DOI 10.1093/pnasnexus/pgad068
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  8. Article: A Molecular Lid Mechanism of K+ Channel Blocker Action Revealed by a Cone Peptide

    Saikia, Chandamita / Dym, Orly / Altman-Gueta, Hagit / Gordon, Dalia / Reuveny, Eitan / Karbat, Izhar

    Journal of molecular biology. 2021 Mar. 16,

    2021  

    Abstract: Many venomous organisms carry in their arsenal short polypeptides that block K⁺ channels in a highly selective manner. These toxins may compete with the permeating ions directly via a “plug” mechanism or indirectly via a “pore-collapse” mechanism. An ... ...

    Abstract Many venomous organisms carry in their arsenal short polypeptides that block K⁺ channels in a highly selective manner. These toxins may compete with the permeating ions directly via a “plug” mechanism or indirectly via a “pore-collapse” mechanism. An alternative “lid” mechanism was proposed but remained poorly defined. Here we study the Drosophila Shaker channel block by Conkunitzin-S1 and Conkunitzin-C3, two highly similar toxins derived from cone venom. Despite their similarity, the two peptides exhibited differences in their binding poses and biophysical assays, implying discrete action modes. We show that while Conkunitzin-S1 binds tightly to the channel turret and acts via a “pore-collapse” mechanism, Conkunitzin-C3 does not contact this region. Instead, Conk-C3 uses a non-conserved Arg to divert the permeant ions and trap them in off-axis cryptic sites above the SF, a mechanism we term a “molecular-lid”. Our study provides an atomic description of the “lid” K⁺ blocking mode and offers valuable insights for the design of therapeutics based on venom peptides.
    Keywords Drosophila ; molecular biology ; polypeptides ; potassium channels ; therapeutics ; venoms
    Language English
    Dates of publication 2021-0316
    Publishing place Elsevier Ltd
    Document type Article
    Note NAL-AP-2-clean ; Pre-press version
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2021.166957
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    Z 4' 63/108: Show issues

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  9. Article ; Online: Shaker-IR K+ channel gating in heavy water: Role of structural water molecules in inactivation.

    Szanto, Tibor G / Gaal, Szabolcs / Karbat, Izhar / Varga, Zoltan / Reuveny, Eitan / Panyi, Gyorgy

    The Journal of general physiology

    2021  Volume 153, Issue 6

    Abstract: It has been reported earlier that the slow (C-type) inactivated conformation in Kv channels is stabilized by a multipoint hydrogen-bond network behind the selectivity filter. Furthermore, MD simulations revealed that structural water molecules are also ... ...

    Abstract It has been reported earlier that the slow (C-type) inactivated conformation in Kv channels is stabilized by a multipoint hydrogen-bond network behind the selectivity filter. Furthermore, MD simulations revealed that structural water molecules are also involved in the formation of this network locking the selectivity filter in its inactive conformation. We found that the application of an extracellular, but not intracellular, solution based on heavy water (D2O) dramatically slowed entry into the slow inactivated state in Shaker-IR mutants (T449A, T449A/I470A, and T449K/I470C, displaying a wide range of inactivation kinetics), consistent with the proposed effect of the dynamics of structural water molecules on the conformational stability of the selectivity filter. Alternative hypotheses capable of explaining the observed effects of D2O were examined. Increased viscosity of the external solution mimicked by the addition of glycerol had a negligible effect on the rate of inactivation. In addition, the inactivation time constants of K+ currents in the outward and the inward directions in asymmetric solutions were not affected by a H2O/D2O exchange, negating an indirect effect of D2O on the rate of K+ rehydration. The elimination of the nonspecific effects of D2O on our macroscopic current measurements supports the hypothesis that the rate of structural water exchange at the region behind the selectivity filter determines the rate of slow inactivation, as proposed by molecular modeling.
    MeSH term(s) Deuterium Oxide ; Hydrogen Bonding ; Ion Channel Gating ; Kinetics ; Water
    Chemical Substances Water (059QF0KO0R) ; Deuterium Oxide (J65BV539M3)
    Language English
    Publishing date 2021-05-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3118-5
    ISSN 1540-7748 ; 0022-1295
    ISSN (online) 1540-7748
    ISSN 0022-1295
    DOI 10.1085/jgp.202012742
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  10. Article ; Online: A Molecular Lid Mechanism of K

    Saikia, Chandamita / Dym, Orly / Altman-Gueta, Hagit / Gordon, Dalia / Reuveny, Eitan / Karbat, Izhar

    Journal of molecular biology

    2021  Volume 433, Issue 17, Page(s) 166957

    Abstract: Many venomous organisms carry in their arsenal short polypeptides that block ... ...

    Abstract Many venomous organisms carry in their arsenal short polypeptides that block K
    MeSH term(s) Amino Acid Sequence ; Animals ; Binding Sites/drug effects ; Biophysics/methods ; Ion Channel Gating/drug effects ; Peptides/pharmacology ; Potassium/metabolism ; Potassium Channels/metabolism ; Scorpion Venoms/pharmacology ; Xenopus laevis/metabolism
    Chemical Substances Peptides ; Potassium Channels ; Scorpion Venoms ; Potassium (RWP5GA015D)
    Language English
    Publishing date 2021-03-24
    Publishing country England
    Document type Journal Article ; 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.2021.166957
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