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Dynamic ion channel defies dogma

It is well established that proteins in the TRP family of ion channels assemble from four subunits. But do they always do this? A five-subunit structure has now been observed, and might be involved in channel regulation.
  1. Ute A. Hellmich

    1. Ute A. Hellmich is in the Faculty of Chemistry and Earth Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, Friedrich Schiller University Jena, 07743 Jena, Germany; the Cluster of Excellence Balance of the Microverse, Friedrich Schiller University Jena; and at the Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University, Frankfurt, Germany.

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Receptor proteins in cell membranes are responsible for sensing signals such as temperature, pressure and the compounds that give foods their pungency — such as the ‘heat’ of spices or the ‘coolness’ of mint. A prominent group of receptors are the ion channels, which include the transient receptor potential (TRP) channels. The first high-resolution structure of a TRP channel was reported1 in 2013 and hundreds more have since been determined2, establishing a common core architecture: four subunits assemble to form a central pore that dilates or constricts in response to stimuli, thus modulating ion flux across cellular membranes. However, writing in Nature, Lansky et al.3 now provide the first evidence that TRP channels can also form from five subunits — prompting the question of whether these pentameric structures are involved in a previously unknown layer of TRP-channel regulation.

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Nature 621, 46-47 (2023)

doi: https://doi.org/10.1038/d41586-023-02486-9

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Competing Interests

The author declares no competing interests.

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