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  The biophysical, molecular, and anatomical landscape of pigeon CRY4: A candidate light-based quantal magnetosensor

Hochstoeger, T., Al Said, T., Maestre, D., Walter, F., Vilceanu, A., Pedron, M., et al. (2020). The biophysical, molecular, and anatomical landscape of pigeon CRY4: A candidate light-based quantal magnetosensor. Science Advances, 6(33): eabb9110. doi:10.1126/sciadv.abb9110.

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Hochstoeger, Tobias1, Author
Al Said, Tarek1, Author
Maestre, Dante1, Author
Walter, Florian1, Author
Vilceanu, Alexandra1, Author
Pedron, Miriam1, Author
Cushion, Thomas D.1, Author
Snider, William1, Author
Nimpf, Simon1, Author
Nordmann, Gregory Charles1, Author
Landler, Lukas1, Author
Edelman, Nathaniel1, Author
Kruppa, Lennard1, Author
Duernberger, Gerhard1, Author
Mechtler, Karl1, Author
Schuechner, Stefan1, Author
Ogris, Egon1, Author
Malkemper, E. Pascal2, Author           
Weber, Stefan1, Author
Schleicher, Erik1, Author
Keays, David A.1, Author more..
Affiliations:
1external, ou_persistent22              
2Max Planck Research Group Neurobiology of Magnetoreception, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_3169318              

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Free keywords: CORRELATED RADICAL PAIRS; DEPENDENT MAGNETORECEPTION; CRYPTOCHROME; PROTEINS; EXPRESSION; MECHANISM; LOCALIZATION; WAVELENGTHS; TRYPTOPHAN; RESONANCE
 Abstract: The biophysical and molecular mechanisms that enable animals to detect magnetic fields are unknown. It has been proposed that birds have a light-dependent magnetic compass that relies on the formation of radical pairs within cryptochrome molecules. Using spectroscopic methods, we show that pigeon cryptochrome clCRY4 is photoreduced efficiently and forms long-lived spin-correlated radical pairs via a tetrad of tryptophan residues. We report that clCRY4 is broadly and stably expressed within the retina but enriched at synapses in the outer plexiform layer in a repetitive manner. A proteomic survey for retinal-specific clCRY4 interactors identified molecules that are involved in receptor signaling, including glutamate receptor-interacting protein 2, which colocalizes with clCRY4. Our data support a model whereby clCRY4 acts as an ultraviolet-blue photoreceptor and/or a light-dependent magnetosensor by modulating glutamatergic synapses between horizontal cells and cones.

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Language(s): eng - English
 Dates: 2020-08-12
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000560465800037
DOI: 10.1126/sciadv.abb9110
PMID: 32851187
 Degree: -

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Title: Science Advances
  Abbreviation : Sci Adv
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 6 (33) Sequence Number: eabb9110 Start / End Page: - Identifier: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548