Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein

Background: Night-migratory birds sense the Earth’s magnetic field by an unknown molecular mechanism. Theoretical and experimental evidence support the hypothesis that the light-induced formation of a radical-pair in European robin cryptochrome 4a (ErCry4a) is the primary signaling step in the retin...

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Main Authors: Katharina Görtemaker, Chad Yee, Rabea Bartölke, Heide Behrmann, Jan-Oliver Voß, Jessica Schmidt, Jingjing Xu, Vita Solovyeva, Bo Leberecht, Elmar Behrmann, Henrik Mouritsen, Karl-Wilhelm Koch
Format: Article
Language:English
Published: MDPI AG 2022-06-01
Series:Cells
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Online Access:https://www.mdpi.com/2073-4409/11/13/2043
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author Katharina Görtemaker
Chad Yee
Rabea Bartölke
Heide Behrmann
Jan-Oliver Voß
Jessica Schmidt
Jingjing Xu
Vita Solovyeva
Bo Leberecht
Elmar Behrmann
Henrik Mouritsen
Karl-Wilhelm Koch
author_facet Katharina Görtemaker
Chad Yee
Rabea Bartölke
Heide Behrmann
Jan-Oliver Voß
Jessica Schmidt
Jingjing Xu
Vita Solovyeva
Bo Leberecht
Elmar Behrmann
Henrik Mouritsen
Karl-Wilhelm Koch
author_sort Katharina Görtemaker
collection DOAJ
description Background: Night-migratory birds sense the Earth’s magnetic field by an unknown molecular mechanism. Theoretical and experimental evidence support the hypothesis that the light-induced formation of a radical-pair in European robin cryptochrome 4a (ErCry4a) is the primary signaling step in the retina of the bird. In the present work, we investigated a possible route of cryptochrome signaling involving the α-subunit of the cone-secific 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 living cells and might constitute the first biochemical signaling step in radical-pair-based magnetoreception.
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spelling doaj.art-e18ee1cb8df64c8ba45b338fca3d87b52023-11-23T19:48:33ZengMDPI AGCells2073-44092022-06-011113204310.3390/cells11132043Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-ProteinKatharina Görtemaker0Chad Yee1Rabea Bartölke2Heide Behrmann3Jan-Oliver Voß4Jessica Schmidt5Jingjing Xu6Vita Solovyeva7Bo Leberecht8Elmar Behrmann9Henrik Mouritsen10Karl-Wilhelm Koch11Division of Biochemistry, Department of Neuroscience, University of Oldenburg, D-26111 Oldenburg, GermanyDivision of Biochemistry, Department of Neuroscience, University of Oldenburg, D-26111 Oldenburg, GermanyAnimal Navigation, Institute of Biology and Environmental Sciences, University of Oldenburg, D-26111 Oldenburg, GermanyInstitute of Biochemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, D-50674 Cologne, GermanyDivision of Biochemistry, Department of Neuroscience, University of Oldenburg, D-26111 Oldenburg, GermanyAnimal Navigation, Institute of Biology and Environmental Sciences, University of Oldenburg, D-26111 Oldenburg, GermanyAnimal Navigation, Institute of Biology and Environmental Sciences, University of Oldenburg, D-26111 Oldenburg, GermanyInstitute of Physics, University of Oldenburg, D-26111 Oldenburg, GermanyAnimal Navigation, Institute of Biology and Environmental Sciences, University of Oldenburg, D-26111 Oldenburg, GermanyInstitute of Biochemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, D-50674 Cologne, GermanyAnimal Navigation, Institute of Biology and Environmental Sciences, University of Oldenburg, D-26111 Oldenburg, GermanyDivision of Biochemistry, Department of Neuroscience, University of Oldenburg, D-26111 Oldenburg, GermanyBackground: Night-migratory birds sense the Earth’s magnetic field by an unknown molecular mechanism. Theoretical and experimental evidence support the hypothesis that the light-induced formation of a radical-pair in European robin cryptochrome 4a (ErCry4a) is the primary signaling step in the retina of the bird. In the present work, we investigated a possible route of cryptochrome signaling involving the α-subunit of the cone-secific 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 living cells and might constitute the first biochemical signaling step in radical-pair-based magnetoreception.https://www.mdpi.com/2073-4409/11/13/2043magnetoreceptioncryptochromeG protein α-subunitprotein-protein interaction
spellingShingle Katharina Görtemaker
Chad Yee
Rabea Bartölke
Heide Behrmann
Jan-Oliver Voß
Jessica Schmidt
Jingjing Xu
Vita Solovyeva
Bo Leberecht
Elmar Behrmann
Henrik Mouritsen
Karl-Wilhelm Koch
Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
Cells
magnetoreception
cryptochrome
G protein α-subunit
protein-protein interaction
title Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
title_full Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
title_fullStr Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
title_full_unstemmed Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
title_short Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
title_sort direct interaction of avian cryptochrome 4 with a cone specific g protein
topic magnetoreception
cryptochrome
G protein α-subunit
protein-protein interaction
url https://www.mdpi.com/2073-4409/11/13/2043
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