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Fenollar nackt Cristina Structural relationship

The transmembrane channel-like 1 TMC1 protein localizes to the site of the MET channel, interacts with the tip-link responsible for mechanical gating, and genetic alterations in TMC1 alter MET channel properties and cause deafness, supporting the hypothesis that TMC1 forms the MET channel.

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A Confocal images displaying 3 kDa dextran-TR fluorescence magenta in top panels at the cell body and stereocilia counterstained with phalloidin to label F-actin green and thereby visualize hair cell boundaries and stereocilia.

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Structural relationship between the putative hair cell mechanotransduction channel TMC1 and TMEM16 proteins

Neighboring IHC, cuticular plate CP and supporting cells SP vesicles V are also indicated.

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1 Molecular Physiology and Biophysics Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.

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PLD2

Each dot represents a single hair cell, and mean and standard deviation for each condition are shown.

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C nhTMEM16 PDB ID: 4WIS and mTMEM16A PDB ID: 5OYB structural alignment obtained with TMalign.

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Tip-link integrity and mechanical transduction in vertebrate hair cells.

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Plasma membrane position is indicated by black lines and the extracellular EC and intracellular IC sides are labeled.

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B Relative fluorescence intensity RFI profile for each protein green and F-actin magenta across the edge of each cell from the extracellular to the intracellular side white line in A.

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Admin30.07.2021

PLD2

The helices of the other protomer are represented as cylinders and the deafness-causing mutations are labeled and indicated as magenta spheres.

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