9ZIT

C. elegans PEZO-1 Isoform K

Summary for 9ZIT

• Entry DOI: 10.2210/pdb9zit/pdb
• EMDB information: 74283
• Descriptor: Piezo-type mechanosensitive ion channel component 1 (1 entity in total)
• Functional Keywords: pezo-1, piezo channels, membrane protein, mechanosensitive ion channels, c. elegans, isoforms
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 3
• Total formula weight: 575437.73

Authors

Bell, B.,Baker, M.L.,Vasquez, V. (deposition date: 2025-12-04, release date: 2025-12-24, Last modification date: 2026-01-21)

Primary citation

Bell, B.,Jaramillo-Granada, A.M.,Orlin, D.J.,Weng, W.H.,Wen, H.,Sotomayor, M.,Chesler, A.T.,Baker, M.L.,Cordero-Morales, J.F.,Vasquez, V.
Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade.
Cell Rep, 45:116878-116878, 2025

PubMed Abstract: PIEZO channels are mechanosensitive ion channels conserved from plants to humans, yet structures exist for only a few mammalian orthologs. We define the structural and functional diversity of Caenorhabditis elegans PEZO-1, a single gene with extensive alternative splicing, by determining cryo-electron microscopy structures of three representative isoforms: G (full length), K (lacking the pore-distal N-terminal blade), and L (missing most of the blade). PEZO-1G displays mechanically evoked currents yet adopts a compact, semi-flattened conformation that significantly differs from the mammalian domes. The blades exhibit a three-step slope architecture stabilized by inter-blade latching among transmembrane helical units, yielding a circular, steering-wheel-like arrangement. A wider cap enables distinct blade-cap contacts that stabilize a "toggle-down" conformation. Isoform K also exhibits mechanically evoked currents, indicating that the pore-distal N-terminal blade is dispensable for mechanoactivation. Computational membrane-deformation modeling indicates that the isoforms impose distinct curvatures on the bilayer. Our findings indicate an evolutionarily distinct architecture for PEZO-1.

PubMed: 41477764
DOI: 10.1016/j.celrep.2025.116878

Experimental method

ELECTRON MICROSCOPY (3.1 Å)