期刊
CELL
卷 162, 期 6, 页码 1391-1403出版社
CELL PRESS
DOI: 10.1016/j.cell.2015.08.024
关键词
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资金
- DFG [SPP 1608 GO 1092/2-1, GO 1092/1-2, SFB 889 A1]
- BRAINseed award
- NIH [R37NS040929, 5R01MH084234]
Howmetazoanmechanotransduction channels sense mechanical stimuli is not well understood. The NOMPC channel in the transient receptor potential (TRP) family, a mechanotransduction channel for Drosophila touch sensation and hearing, contains 29 Ankyrin repeats (ARs) that associate with microtubules. These ARs have been postulated to act as a tether that conveys force to the channel. Here, we report that these N-terminal ARs form a cytoplasmicdomain essential forNOMPC mechanogating in vitro, mechanosensitivity of touch receptor neurons in vivo, and touch-induced behaviors of Drosophila larvae. Duplicating the ARs elongates the filaments that tether NOMPC to microtubules in mechanosensory neurons. Moreover, microtubule association is required for NOMPC mechanogating. Importantly, transferring the NOMPC ARs to mechanoinsensitive voltage-gated potassium channels confers mechanosensitivity to the chimeric channels. These experiments strongly support a tethermechanismofmechanogating for the NOMPC channel, providing insights into the basis ofmechanosensitivity ofmechanotransduction channels.
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