8IMZ
Cryo-EM structure of mouse Piezo1-MDFIC complex (composite map)
Summary for 8IMZ
| Entry DOI | 10.2210/pdb8imz/pdb |
| EMDB information | 35577 36241 36242 36243 36244 |
| Descriptor | Piezo-type mechanosensitive ion channel component 1, MyoD family inhibitor domain-containing protein (2 entities in total) |
| Functional Keywords | piezo1 complex, mechanosensation, mechanotransduction, membrane protein |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 6 |
| Total formula weight | 955330.16 |
| Authors | |
| Primary citation | Zhou, Z.,Ma, X.,Lin, Y.,Cheng, D.,Bavi, N.,Secker, G.A.,Li, J.V.,Janbandhu, V.,Sutton, D.L.,Scott, H.S.,Yao, M.,Harvey, R.P.,Harvey, N.L.,Corry, B.,Zhang, Y.,Cox, C.D. MyoD-family inhibitor proteins act as auxiliary subunits of Piezo channels. Science, 381:799-804, 2023 Cited by PubMed Abstract: Piezo channels are critical cellular sensors of mechanical forces. Despite their large size, ubiquitous expression, and irreplaceable roles in an ever-growing list of physiological processes, few Piezo channel-binding proteins have emerged. In this work, we found that MyoD (myoblast determination)-family inhibitor proteins (MDFIC and MDFI) are PIEZO1/2 interacting partners. These transcriptional regulators bind to PIEZO1/2 channels, regulating channel inactivation. Using single-particle cryogenic electron microscopy, we mapped the interaction site in MDFIC to a lipidated, C-terminal helix that inserts laterally into the PIEZO1 pore module. These Piezo-interacting proteins fit all the criteria for auxiliary subunits, contribute to explaining the vastly different gating kinetics of endogenous Piezo channels observed in many cell types, and elucidate mechanisms potentially involved in human lymphatic vascular disease. PubMed: 37590348DOI: 10.1126/science.adh8190 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.66 Å) |
Structure validation
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