Article
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Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-protein
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Version 1
: Received: 13 June 2022 / Approved: 14 June 2022 / Online: 14 June 2022 (08:37:43 CEST)
A peer-reviewed article of this Preprint also exists.
Görtemaker et al. Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein. Cells 2022, 11, 2043. Görtemaker et al. Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein. Cells 2022, 11, 2043.
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.
Keywords
magnetoreception; cryptochrome; G protein α-subunit; protein-protein interaction
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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