Grammitidoideae are the largest subfamily in Polypodiaceae and contain about 911 species. Progress has been made in understanding the overall phylogeny and generic boundaries in the light of recent molecular works. However, the majority of species, especially Asian species, and some critical type species of genera remain unsampled. In this study, a dataset of six plastid markers of 1003 (112 new) accessions representing ca. 412 species of Grammitidoideae including the type species of Ctenopterella, Grammitis, Moranopteris, Radiogrammitis, and Themelium, was assembled to infer a phylogeny. Our major results include: (1) the type species of Grammitis is successfully sequenced using a next‐generation sequencing technique and is resolved in Grammitis s.str. as expected; (2) Ctenopterella is found to be polyphyletic and a new clade consisting of C. khaoluangensis is resolved as sister to Tomophyllum; (3) the type species of Ctenopterella is resolved in a clade sister to the C. lasiostipes clade; (4) Oreogrammitis is found to be polyphyletic and three clades outside of the core Oreogrammitis are identified containing O. subevenosa and allies, O. orientalis, and O. beddomeana (+ O. cf. beddomeana); (5) Prosaptia is found to be paraphyletic with P. nutans being sister to a clade containing the rest of Prosaptia and Archigrammitis; (6) the intergeneric and major relationships within the Asia‐Pacific clade are well resolved and strongly supported except for a few branches; (7) extensive cryptic speciation is detected in the Asia‐Pacific clade; and (8) based on the polyphyly of Ctenopterella we describe three new genera, Boonkerdia, Oxygrammitis, and Rouhania, for species formerly in Ctenopterella; because the type species of Grammitis belongs to Grammitis s.str., we describe five new genera, Aenigmatogrammitis, Grammitastrum (stat. nov.), Howeogrammitis, Nanogrammitis, and Thalassogrammitis for species formerly in Grammitis s.l. A key to the 35 Old‐World genera is given, a taxonomic treatment is presented, and the morphology of all new genera is shown with either a color plate and/or a line drawing.
Transient receptor potential A1 (TRPA1) is implicated in somatosensory processing and pathological pain sensation. Although not strictly voltage-gated, ionic currents of TRPA1 typically rectify outwardly, indicating channel activation at depolarized membrane potentials. However, some reports also showed TRPA1 inactivation at high positive potentials, implicating voltage-dependent inactivation. Here we report a conserved leucine residue, L906, in the putative pore helix, which strongly impacts the voltage dependency of TRPA1. Mutation of the leucine to cysteine (L906C) converted the channel from outward to inward rectification independent of divalent cations and irrespective to stimulation by allyl isothiocyanate. The mutant, but not the wild-type channel, displayed exclusively voltage-dependent inactivation at positive potentials. The L906C mutation also exhibited reduced sensitivity to inhibition by TRPA1 blockers, HC030031 and ruthenium red. Further mutagenesis of the leucine to all natural amino acids individually revealed that most substitutions at L906 (15/19) resulted in inward rectification, with exceptions of three amino acids that dramatically reduced channel activity and one, methionine, which mimicked the wild-type channel. Our data are plausibly explained by a bimodal gating model involving both voltage-dependent activation and inactivation of TRPA1. We propose that the key pore helix residue, L906, plays an essential role in responding to the voltage-dependent gating.
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