Peng Guangda, Kashio Makiko, Li Tianbang, Dong Xiaofeng, Tominaga Makoto, Kadowaki Tatsuhiko
Department of Biological Sciences, Xi'an Jiaotong-Liverpool University Suzhou, China.
Division of Cell Signaling, Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences Okazaki, Japan.
Front Physiol. 2016 Oct 5;7:447. doi: 10.3389/fphys.2016.00447. eCollection 2016.
The transient receptor potential cation channel, subfamily A, member 1 (TRPA1) is conserved between many arthropods, and in some has been shown to function as a chemosensor for noxious compounds. Activation of arthropod TRPA1 channels by temperature fluctuations has been tested in only a few insect species, and all of them were shown to be activated by heat. The recent identification of chemosensitive TRPA1 channels from two honey bee ectoparasitic mite species (VdTRPA1 and TmTRPA1) have provided an opportunity to study the temperature-dependent activation and the temperature-associated physiological functions of TRPA1 channels in non-insect arthropods. We found that both mite TRPA1 channels are heat sensitive and capable of rescuing the temperature-related behavioral defects of a mutant. These results suggest that heat-sensitivity of TRPA1 could be conserved between many arthropods despite its amino acid sequence diversity. Nevertheless, the ankyrin repeats (ARs) 6 and 7 are well-conserved between six heat-sensitive arthropod TRPA1 channels and have critical roles for the heat activation of VdTRPA1.
瞬时受体电位阳离子通道A亚家族成员1(TRPA1)在许多节肢动物中保守,并且在一些节肢动物中已被证明可作为有害化合物的化学传感器。仅在少数昆虫物种中测试了温度波动对节肢动物TRPA1通道的激活作用,并且所有这些物种都显示可被热激活。最近从两种蜜蜂体外寄生螨物种(VdTRPA1和TmTRPA1)中鉴定出化学敏感的TRPA1通道,为研究非昆虫节肢动物中TRPA1通道的温度依赖性激活和与温度相关的生理功能提供了机会。我们发现两种螨类TRPA1通道均对热敏感,并且能够挽救突变体与温度相关的行为缺陷。这些结果表明,尽管TRPA1的氨基酸序列存在多样性,但在许多节肢动物中TRPA1的热敏感性可能是保守的。然而,锚蛋白重复序列(ARs)6和7在六个热敏感节肢动物TRPA1通道之间高度保守,并且对VdTRPA1的热激活起关键作用。