Structure and function of plant photoreceptors
Abstract
Signaling photoreceptors use the information contained in the absorption of a photon to modulate biological activity in plants and a wide range of organisms. The fundamental-and as yet imperfectly answered-question is, how is this achieved at the molecular level? We adopt the perspective of biophysicists interested in light-dependent signal transduction in nature and the three-dimensional structures that underpin signaling. Six classes of photoreceptors are known: light-oxygen-voltage (LOV) sensors, xanthopsins, phytochromes, blue-light sensors using flavin adenine dinucleotide (BLUF), cryptochromes, and rhodopsins. All are water-soluble proteins except rhodopsins, which are integral membrane proteins; all are based on a modular architecture except cryptochromes and rhodopsins; and each displays a distinct, light-dependent chemical process based on the photochemistry of their nonprotein chromophore, such as isomerization about a double bond (xanthopsins, phytochromes, and rhodopsins), formation or rupture of a covalent bond (LOV sensors), or electron transfer (BLUF sensors and cryptochromes).
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In plants, plant-type Cryptochromes function as photoreceptors for the plant circadian clock.
“In plants, members of this family have been shown to function as photoreceptors for the plant circadian clock [reviewed in Ref. (38)].”
From An Overview of Monthly Rhythms and Clocks (2017) · cites this paper as [38]
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An Overview of Monthly Rhythms and Clocks
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The cryptochrome/photolyase family in aquatic organisms
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- Authors
- Möglich, A., Yang, X., Ayers, R. A., & Moffat, K.
- Affiliations
- University of Chicago (US)
- Venue
- Annual Review of Plant Biology
- Publisher
- Annual Reviews
- Published
- 2010-06-02
- Volume
- 61
- Issue
- 1
- Pages
- 21-47
- ISSN
- 1543-5008 (ISSN-L)
- 1545-2123
- OpenAlex
- W2157889657
- Cited by
- 499
- References
- 168
- Citations by year
- 2026: 13 · 2025: 15 · 2024: 33 · 2023: 28 · 2022: 34 · 2021: 39 · 2020: 29 · 2019: 33 · 2018: 26 · 2017: 35 · 2016: 40 · 2015: 32 · 2014: 42 · 2013: 29 · 2012: 32
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Plant Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM036452)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- plant photoreceptors, light signaling, phytochrome, BLUF protein, cryptochrome, rhodopsin, protein structure, flavin adenine dinucleotide, covalent bond formation, electron transfer
- MeSH terms
- Models, Molecular, Photochemistry, Signal Transduction, Photoreceptors, Plant
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