6LQI
Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1
Summary for 6LQI
| Entry DOI | 10.2210/pdb6lqi/pdb |
| EMDB information | 0946 |
| Descriptor | Piezo-type mechanosensitive ion channel component 1 (1 entity in total) |
| Functional Keywords | piezo1.1, mechanogating, mechanotransduction channel, membrane protein, isoform |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 3 |
| Total formula weight | 868771.88 |
| Authors | |
| Primary citation | Geng, J.,Liu, W.,Zhou, H.,Zhang, T.,Wang, L.,Zhang, M.,Li, Y.,Shen, B.,Li, X.,Xiao, B. A Plug-and-Latch Mechanism for Gating the Mechanosensitive Piezo Channel. Neuron, 106:438-, 2020 Cited by PubMed Abstract: The mechanosensitive Piezo1 and Piezo2 channels convert mechanical force into cation permeation. However, their precise mechanogating and regulatory mechanisms remain elusive. Here, we report that Piezo1 utilizes three lateral ion-conducting portals equipped with physical gates for cooperative gating and splicing regulation. Mutating residues lining the portal converts Piezo1 into an anion-selective channel, demonstrating the portal-based cation-permeating pathway. Intriguingly, the portal is physically blocked with a plug domain, which undergoes alternative splicing in both Piezo1 and Piezo2. The Piezo1 isoform has local openings of the portals, enlarged single-channel conductance and sensitized mechanosensitivity. Remarkably, the three plugs are strategically latched onto the central axis for coordinated gating of the three portals. Disrupting the latching induces three quantal sub-conductance states in Piezo1, but not in the isoform. Together, we propose that Piezo utilizes an elegant plug-and-latch mechanism to physically and coordinately gate the lateral portals through the spliceable plug gates. PubMed: 32142647DOI: 10.1016/j.neuron.2020.02.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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