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TMHS Is an Integral Component of the Mechanotransduction Machinery of Cochlear Hair Cells

Xiong, Wei ; Grillet, Nicolas ; Elledge, Heather M. ; Wagner, Thomas F.J. ; Zhao, Bo ; Johnson, Kenneth R. ; Kazmierczak, Piotr ; Müller, Ulrich

Cell, 2012-12, Vol.151 (6), p.1283-1295 [Periódico revisado por pares]

United States: Elsevier Inc

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  • Título:
    TMHS Is an Integral Component of the Mechanotransduction Machinery of Cochlear Hair Cells
  • Autor: Xiong, Wei ; Grillet, Nicolas ; Elledge, Heather M. ; Wagner, Thomas F.J. ; Zhao, Bo ; Johnson, Kenneth R. ; Kazmierczak, Piotr ; Müller, Ulrich
  • Assuntos: Adaptations ; Animals ; Cadherins - metabolism ; cells ; Hair Cells, Auditory - metabolism ; Hearing ; ion channels ; mechanotransduction ; Mechanotransduction, Cellular ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membrane Proteins - ultrastructure ; Mice ; Mice, Knockout ; mutation ; propionic acid ; Protein Precursors - metabolism ; receptors ; regulatory proteins ; Stereocilia - metabolism
  • É parte de: Cell, 2012-12, Vol.151 (6), p.1283-1295
  • Notas: http://dx.doi.org/10.1016/j.cell.2012.10.041
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  • Descrição: Hair cells are mechanosensors for the perception of sound, acceleration, and fluid motion. Mechanotransduction channels in hair cells are gated by tip links, which connect the stereocilia of a hair cell in the direction of their mechanical sensitivity. The molecular constituents of the mechanotransduction channels of hair cells are not known. Here, we show that mechanotransduction is impaired in mice lacking the tetraspan TMHS. TMHS binds to the tip-link component PCDH15 and regulates tip-link assembly, a process that is disrupted by deafness-causing Tmhs mutations. TMHS also regulates transducer channel conductance and is required for fast channel adaptation. TMHS therefore resembles other ion channel regulatory subunits such as the transmembrane alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptor regulatory proteins (TARPs) of AMPA receptors that facilitate channel transport and regulate the properties of pore-forming channel subunits. We conclude that TMHS is an integral component of the hair cell’s mechanotransduction machinery that functionally couples PCDH15 to the transduction channel. [Display omitted] ► TMHS is a component of the hair cell’s mechanotransduction machinery ► TMHS binds to the tip-link component PCDH15 and regulates tip-link assembly ► TMHS regulates transducer channel conductance and is required for adaptation ► TMHS is structurally similar to other ion channel regulatory subunits such as TARPs The tetraspan TMHS is identified as an accessory subunit of the hair cell mechanotransducer channel. TMHS regulates transducer channel conductance and functionally couples the tip-link component protocadherin 15 to the transduction channel.
  • Editor: United States: Elsevier Inc
  • Idioma: Inglês
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