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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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Autores principales: Görtemaker, Katharina, Yee, Chad, Bartölke, Rabea, Behrmann, Heide, Voß, Jan-Oliver, Schmidt, Jessica, Xu, Jingjing, Solovyeva, Vita, Leberecht, Bo, Behrmann, Elmar, Mouritsen, Henrik, Koch, Karl-Wilhelm
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9265643/
https://www.ncbi.nlm.nih.gov/pubmed/35805127
http://dx.doi.org/10.3390/cells11132043
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author Görtemaker, Katharina
Yee, Chad
Bartölke, Rabea
Behrmann, Heide
Voß, Jan-Oliver
Schmidt, Jessica
Xu, Jingjing
Solovyeva, Vita
Leberecht, Bo
Behrmann, Elmar
Mouritsen, Henrik
Koch, Karl-Wilhelm
author_facet Görtemaker, Katharina
Yee, Chad
Bartölke, Rabea
Behrmann, Heide
Voß, Jan-Oliver
Schmidt, Jessica
Xu, Jingjing
Solovyeva, Vita
Leberecht, Bo
Behrmann, Elmar
Mouritsen, Henrik
Koch, Karl-Wilhelm
author_sort Görtemaker, Katharina
collection PubMed
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 pubmed-92656432022-07-09 Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein Görtemaker, Katharina Yee, Chad Bartölke, Rabea Behrmann, Heide Voß, Jan-Oliver Schmidt, Jessica Xu, Jingjing Solovyeva, Vita Leberecht, Bo Behrmann, Elmar Mouritsen, Henrik Koch, Karl-Wilhelm Cells Article 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. MDPI 2022-06-27 /pmc/articles/PMC9265643/ /pubmed/35805127 http://dx.doi.org/10.3390/cells11132043 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Görtemaker, Katharina
Yee, Chad
Bartölke, Rabea
Behrmann, Heide
Voß, Jan-Oliver
Schmidt, Jessica
Xu, Jingjing
Solovyeva, Vita
Leberecht, Bo
Behrmann, Elmar
Mouritsen, Henrik
Koch, Karl-Wilhelm
Direct Interaction of Avian Cryptochrome 4 with a Cone Specific G-Protein
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 Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9265643/
https://www.ncbi.nlm.nih.gov/pubmed/35805127
http://dx.doi.org/10.3390/cells11132043
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