Sequence variations and accessory proteins adapt TMC functions to distinct sensory modalities.
Neuron
; 112(17): 2922-2937.e8, 2024 Sep 04.
Article
in En
| MEDLINE
| ID: mdl-38986620
ABSTRACT
Transmembrane channel-like (TMC) proteins are expressed throughout the animal kingdom and are thought to encode components of ion channels. Mammals express eight TMCs (mTMC1-8), two of which (mTMC1 and mTMC2) are subunits of mechanotransduction channels. C. elegans expresses two TMCs (TMC-1 and TMC-2), which mediate mechanosensation, egg laying, and alkaline sensing. The mechanisms by which nematode TMCs contribute to such diverse physiological processes and their functional relationship to mammalian mTMCs is unclear. Here, we show that association with accessory proteins tunes nematode TMC-1 to divergent sensory functions. In addition, distinct TMC-1 domains enable touch and alkaline sensing. Strikingly, these domains are segregated in mammals between mTMC1 and mTMC3. Consistent with these findings, mammalian mTMC1 can mediate mechanosensation in nematodes, while mTMC3 can mediate alkaline sensation. We conclude that sequence diversification and association with accessory proteins has led to the emergence of TMC protein complexes with diverse properties and physiological functions.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Caenorhabditis elegans
/
Caenorhabditis elegans Proteins
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Mechanotransduction, Cellular
Limits:
Animals
/
Humans
Language:
En
Journal:
Neuron
Journal subject:
NEUROLOGIA
Year:
2024
Document type:
Article
Affiliation country:
Country of publication: