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Journal Article

Structure of tetrameric forms of the serotonin-gated 5-HT3A receptor ion channel

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Introini,  Bianca       
Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society;
Buchmann Institute for Molecular Life Sciences (BMLS), Goethe University of Frankfurt am Main, Frankfurt on Main, Germany;

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Zhang,  Yingyi
Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society;
Buchmann Institute for Molecular Life Sciences (BMLS), Goethe University of Frankfurt am Main, Frankfurt on Main, Germany;

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Eckhardt-Strelau,  Luise
Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society;

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Kudryashev,  Mikhail       
Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society;
Buchmann Institute for Molecular Life Sciences (BMLS), Goethe University of Frankfurt am Main, Frankfurt on Main, Germany;
Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), In Situ Structural Biology, Berlin, Germany;
Institute of Medical Physics and Biophysics, Charité-Universitätsmedizin, Berlin, Germany;

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Citation

Introini, B., Cui, W., Chu, X., Zhang, Y., Alves, A. C., Eckhardt-Strelau, L., et al. (2024). Structure of tetrameric forms of the serotonin-gated 5-HT3A receptor ion channel. The EMBO Journal, 43(20), 4451-4471. doi:10.1038/s44318-024-00191-5.


Cite as: https://hdl.handle.net/21.11116/0000-000F-CD14-4
Abstract
Multimeric membrane proteins are produced in the endoplasmic reticulum and transported to their target membranes which, for ion channels, is typically the plasma membrane. Despite the availability of many fully assembled channel structures, our understanding of assembly intermediates, multimer assembly mechanisms, and potential functions of non-standard assemblies is limited. We demonstrate that the pentameric ligand-gated serotonin 5-HT3A receptor (5-HT3AR) can assemble to tetrameric forms and report the structures of the tetramers in plasma membranes of cell-derived microvesicles and in membrane memetics using cryo-electron microscopy and tomography. The tetrameric structures have near-symmetric transmembrane domains, and asymmetric extracellular domains, and can bind serotonin molecules. Computer simulations, based on our cryo-EM structures, were used to decipher the assembly pathway of pentameric 5-HT3R and suggest a potential functional role for the tetrameric receptors.