Active Cells, Biochemistry & Physiology Genetics & Molecular Biology

Investigating the multiple roles of cryptochromes in animal magnetoreception

In plain English

AI plain-English summary

A protein best known for setting the body’s internal clock may also act as a biological compass, and a fragment of that protein can trigger magnetic responses in fruit flies even without the part scientists thought was essential. This matters because many animals—birds, insects, even humans—are reported to sense magnetic fields, but the mechanism remains disputed. The leading theory involves a quantum reaction inside a protein called cryptochrome, but the researchers have found that a piece of the protein lacking the key chemical machinery still works. That forces a fundamental rethinking of how magnetic sensing might operate at the molecular level. If the team succeeds in mapping the full sensory chain—from detection to behaviour—it would resolve a long-standing puzzle in sensory biology. This is primarily fundamental science: understanding how a living cell detects an invisible physical field. There is no immediate practical application. However, a deeper grasp of magnetoreception could eventually inform bio-inspired navigation systems, improve safety guidelines for electromagnetic field exposure, or reveal unexpected links between circadian rhythms and environmental sensing. Past work on cryptochromes has already reshaped chronobiology; this project could do the same for magnetobiology.

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Many species, including humans, are reported to be magnetosensitive. Indeed, some animals navigate using the weak magnetic field (MF) of Earth. Others do not, but there are accounts of MF-effects and the concern that exposure to low frequency MFs may affect health. Whether the same or different mechanisms may be involved, is currently unknown. One mechanism has acquired experimental prominence. Cryptochromes (CRYs), best known for their role in circadian rhythmicity, may mediate magnetosensitivity via a photochemical quantum reaction involving CRY-bound flavin adenine dinucleotide (FAD) and a chain of tryptophan residues within CRY that generate a radical pair (RP). Unexpectedly, we have demonstrated that the CRY C-terminal (CRY-CT), without the canonical FAD binding site or tryptophan chain, elicits behavioural and cellular responses to MFs in Drosophila melanogaster. Our results do not necessarily contradict the RP model but urge a fundamental revision of its canonical interpretation. We propose a multidisciplinary programme of work examining each level of the sensory chain, including detection, signal transduction and amplification, cellular and behavioural responses. Our combined expertise includes quantum physics, computational chemistry, protein biophysics, electrophysiology, molecular genetics, and behaviour. We are thus uniquely positioned to address and move towards solving this fascinating and fundamental biological question.

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Researchers

Charalambos Kyriacou (EPMC Awardee)

Related Research

Grants with similar aims, by meaning.

Cryptochrome and magnetosensitivity in Drosophila
Exploring Magnetoreception: Radical Motion, Protein Dynamics, and Magnetic Field Effects Across Biological Models
Three, not two, radicals: Revealing the true mechanism of cryptochrome magneto-sensation
Towards the magnetic control of target cells
Quantum Sensing in Nature and Synthetic Biology

Original classification

Discovery Award

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