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- W4282831844 abstract "Background: Night-migratory birds sense the Earth´s magnetic field by an unknown molecular mechanism. Theoretical and experimental evidence support the hypothesis that light-induced formation of a radical-pair in European robin cryptochrome 4a, ErCry4a, is the primary signalling step in the retina of the bird. In the present work, we investigated a possible route of cryptochrome signalling involving the α-subunit of the cone specific heterotrimeric G protein from European robin. Methods: Protein-protein interaction studies include surface plasmon resonance, pulldown affinity binding and Förster resonance energy transfer. Results: Surface plasmon resonance studies showed direct interaction revealing high to moderate affinity for binding of non-myristoylated and myristoylated G protein to ErCry4a, respectively. Pulldown affinity experiments confirmed this complex formation in solution. We validated these in vitro data by monitoring the interaction between ErCry4a and G protein in a transiently transfected neuroretinal cell line using Förster resonance energy transfer. Conclusions: Our results suggest that ErCry4a and the G protein also interact in vivo and might constitute the first biochemical signalling step in radical-pair-based magnetoreception." @default.
- W4282831844 created "2022-06-15" @default.
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- W4282831844 date "2022-06-14" @default.
- W4282831844 modified "2023-09-29" @default.
- W4282831844 title "Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-protein" @default.
- W4282831844 doi "https://doi.org/10.20944/preprints202206.0198.v1" @default.
- W4282831844 hasPublicationYear "2022" @default.
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