Sevastopol, Sevastopol, Russian Federation
Sevastopol, Sevastopol, Russian Federation
Sevastopol, Sevastopol, Russian Federation
A.O. Kovalevsky Institute of Biology of the South Seas of the RAS
Sevastopol State University
Sevastopol, Sevastopol, Russian Federation
Mechanoreceptors can transform external mechanical forces into electrochemical signals that induce cell membrane depolarization and initiate waves propagating along the cell surface. The TRPN1/NompC mechanotransduction channel is known to contain ankyrin repeats that act as a gating helix in Drosophila melanogaster [Jin et al., 2017]. In this work, we present for the first time a family of cationic TRPA1-channels in Trichoplax sp. H2 (Placozoa), which consists of 42 homologs ranging from 468 to 3240 aa in length. Three isolated clusters with different polypeptide chain lengths and various contents of ankyrin repeats were identified within the family. The spatial structure of TRPA1-channel RDD36842.1 was reconstructed, and aspirin, a possible TRP-channel blocker, was docked. The structure of the family members is analyzed, the mechanical model of channel operation is considered, and the probable function and physiology of these protein molecules and their role in the behavior of trichoplax are discussed. Variations in the number of ankyrin repeats at the N-terminus of TRP-proteins studied, and the differences detected at the C-terminus can indicate the polyfunctionality of these proteins in Placozoa. Perhaps TRP channels arose in early evolutionary stages before the appearance of multicellularity, but diversified in multicellular animals as the structural organization of those became more complex.
Placozoa, mechanotransduction, TRP-channels, protein 3D-reconstruction, docking
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