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  • Animals  (2)
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  • 1
    Publikationsdatum: 2001-06-26
    Beschreibung: Outer hair cells (OHCs) of the mammalian cochlea actively change their cell length in response to changes in membrane potential. This electromotility, thought to be the basis of cochlear amplification, is mediated by a voltage-sensitive motor molecule recently identified as the membrane protein prestin. Here, we show that voltage sensitivity is conferred to prestin by the intracellular anions chloride and bicarbonate. Removal of these anions abolished fast voltage-dependent motility, as well as the characteristic nonlinear charge movement ("gating currents") driving the underlying structural rearrangements of the protein. The results support a model in which anions act as extrinsic voltage sensors, which bind to the prestin molecule and thus trigger the conformational changes required for motility of OHCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oliver, D -- He, D Z -- Klocker, N -- Ludwig, J -- Schulte, U -- Waldegger, S -- Ruppersberg, J P -- Dallos, P -- Fakler, B -- DC00089/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 22;292(5525):2340-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology II, University of Tubingen, 72074 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423665" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Substitution ; Animals ; Anion Transport Proteins ; Anions/pharmacology ; Bicarbonates/*metabolism/pharmacology ; CHO Cells ; Cations/pharmacology ; Cell Membrane/metabolism ; Chlorides/*metabolism/pharmacology ; Cricetinae ; Electric Conductivity ; Electrophysiology ; Hair Cells, Auditory, Outer/*physiology ; Models, Biological ; Mutation ; Patch-Clamp Techniques ; Protein Conformation ; Proteins/chemistry/genetics/*metabolism ; Rats
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 2009-03-07
    Beschreibung: Glutamate receptors of the AMPA-subtype (AMPARs), together with the transmembrane AMPAR regulatory proteins (TARPs), mediate fast excitatory synaptic transmission in the mammalian brain. Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. Coassembly with cornichon homologs 2 and 3 affects AMPARs in two ways: Cornichons increase surface expression of AMPARs, and they alter channel gating by markedly slowing deactivation and desensitization kinetics. These results demonstrate that cornichons are intrinsic auxiliary subunits of native AMPARs and provide previously unknown molecular determinants for glutamatergic neurotransmission in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwenk, Jochen -- Harmel, Nadine -- Zolles, Gerd -- Bildl, Wolfgang -- Kulik, Akos -- Heimrich, Bernd -- Chisaka, Osamu -- Jonas, Peter -- Schulte, Uwe -- Fakler, Bernd -- Klocker, Nikolaj -- New York, N.Y. -- Science. 2009 Mar 6;323(5919):1313-9. doi: 10.1126/science.1167852.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology II, University of Freiburg, Engesserstrasse 4, 79108 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19265014" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Brain/cytology/*metabolism ; Cell Membrane/metabolism ; Glutamic Acid/metabolism ; Immunohistochemistry ; *Ion Channel Gating ; Kinetics ; Membrane Proteins/chemistry/metabolism ; Mice ; Neurons/*metabolism ; Patch-Clamp Techniques ; Protein Subunits/chemistry/metabolism ; Proteomics ; Rats ; Receptors, AMPA/chemistry/*metabolism ; Signal Transduction ; Synapses/metabolism ; *Synaptic Transmission ; Xenopus
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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