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7. Introduction

Author

Leidl, R., Potthoff, P., Schwefel, D., Davis, K., editor, van Eimeren, W., editor, Leidl, Reiner, editor, Potthoff, Peter, editor, and Schwefel, Detlef, editor

Published
1990
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16. Effektivitätsmessung von Qualitätssicherungsprogrammen

Author

Schwefel, D., John, J., Potthoff, P., Koller, S., editor, Reichertz, P. L., editor, Überla, K., editor, Anderson, J., editor, Goos, G., editor, Gremy, F., editor, Jesdinsky, H.-J., editor, Lange, H.-J., editor, Schneider, B., editor, Segmüller, G., editor, Wagner, G., editor, Selbmann, Hans-Konrad, editor, Schwartz, Friedrich Wilhelm, editor, and van Eimeren, Wilhelm, editor

Published
1981
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24. Steps to Evaluate a Health Policy

Author

Schwefel, D., Satzinger, W., Potthoff, P., John, J., Davis, K., editor, van Eimeren, W., editor, van Eimeren, Wilhelm, editor, Engelbrecht, Rolf, editor, and Flagle, Charles D., editor

Published
1984
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26. A stomatin dimer modulates the activity of acid-sensing ion channels

Author

Brand, J., Smith, E.S.J., Schwefel, D., Lapatsina, L., Poole, K., Omerbasic, D., Kozlenkov, A., Behlke, J., Lewin, G.R., and Daumke, O.

Subjects
Cancer Research, ASIC, membrane trafficking, Membrane Proteins, Mice, Transgenic, Blood Proteins, CHO Cells, Fibroblasts, Article, Protein Structure, Tertiary, Rats, Acid Sensing Ion Channels, stomatin family, Mice, Cricetulus, HEK293 Cells, Cricetinae, Animals, Humans, protein structure, Function and Dysfunction of the Nervous System, Dimerization, ion channel regulation, Cells, Cultured
Abstract

Stomatins govern membrane trafficking and ion channel activity. The banana-shaped stomatin-domain dimmers oligomerize into a cylindrical structure. A dynamic hydrophobic pocket at the concave side of the dimer mediates repression of acid-sensing ion channel 3 (ASIC3) activity., Stomatin proteins oligomerize at membranes and have been implicated in ion channel regulation and membrane trafficking. To obtain mechanistic insights into their function, we determined three crystal structures of the conserved stomatin domain of mouse stomatin that assembles into a banana-shaped dimer. We show that dimerization is crucial for the repression of acid-sensing ion channel 3 (ASIC3) activity. A hydrophobic pocket at the inside of the concave surface is open in the presence of an internal peptide ligand and closes in the absence of this ligand, and we demonstrate a function of this pocket in the inhibition of ASIC3 activity. In one crystal form, stomatin assembles via two conserved surfaces into a cylindrical oligomer, and these oligomerization surfaces are also essential for the inhibition of ASIC3-mediated currents. The assembly mode of stomatin uncovered in this study might serve as a model to understand oligomerization processes of related membrane-remodelling proteins, such as flotillin and prohibitin.

Published
2012

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