A dynein-associated photoreceptor protein prevents ciliary acclimation to blue light.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 33637535.
- Also identified by DOI 10.1126/sciadv.abf3621 and PMC identifier 7909887.
- Licence recorded as CC BY-NC.
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Abstract
Light-responsive regulation of ciliary motility is known to be conducted through modulation of dyneins, but the mechanism is not fully understood. Here, we report a novel subunit of the two-headed f/I1 inner arm dynein, named DYBLUP, in animal spermatozoa and a unicellular green alga. This subunit contains a BLUF (sensors of blue light using FAD) domain that appears to directly modulate dynein activity in response to light. DYBLUP (dynein-associated BLUF protein) mediates the connection between the f/I1 motor domain and the tether complex that links the motor to the doublet microtubule. <i>Chlamydomonas</i> lacking the DYBLUP ortholog shows both positive and negative phototaxis but becomes acclimated and attracted to high-intensity blue light. These results suggest a mechanism to avoid toxic strong light via direct photoregulation of dyneins.