The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The LOV Domain Family: Photoresponsive Signaling Modules Coupled to Diverse Output Domains
Abstract
For single-cell and multicellular systems to survive, they must accurately sense and respond to their cellular and extracellular environment. Light is a nearly ubiquitous environmental factor, and many species have evolved the capability to respond to this extracellular stimulus. Numerous photoreceptors underlie the activation of light-sensitive signal transduction cascades controlling these responses. Here, we review the properties of the light, oxygen, or voltage (LOV) family of blue-light photoreceptor domains, a subset of the Per-ARNT-Sim (PAS) superfamily. These flavin-binding domains, first identified in the higher-plant phototropins, are now shown to be present in plants, fungi, and bacteria. Notably, LOV domains are coupled to a wide array of other domains, including kinases, phosphodiesterases, F-box domains, STAS domains, and zinc fingers, which suggests that the absorption of blue light by LOV domains regulates the activity of these structurally and functionally diverse domains. LOV domains contain a conserved molecular volume extending from the flavin cofactor, which is the locus for light-driven structural change, to the molecular surface. We discuss the role of this conserved volume of structure in LOV-regulated processes.
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Citations
Cites
PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light
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Novel domains of the prokaryotic two-component signal transduction systems
Galperin, M. (2001) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(01)00326-3 · Cited by 665
The Photocycle of a Flavin-binding Domain of the Blue Light Photoreceptor Phototropin
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Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
Christie, J. M., Swartz, T. E., Bogomolni, R. A., & Briggs, W. R. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.01415.x · Cited by 289
First Evidence for Phototropin-Related Blue-Light Receptors in Prokaryotes
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Structure and Interactions of PAS Kinase N-Terminal PAS Domain
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Key issues in the photochemistry and signalling-state formation of photosensor proteins
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Cited by
Phototropin Blue-Light Receptors
Christie, J. M. (2007) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.58.032806.103951 · Cited by 937
FKF1 and GIGANTEA Complex Formation Is Required for Day-Length Measurement in Arabidopsis
Sawa, M., Nusinow, D. A., Kay, S. A., & Imaizumi, T. (2007) · Science · doi:10.1126/science.1146994 · Cited by 909
Structure and Signaling Mechanism of Per-ARNT-Sim Domains
Möglich, A., Ayers, R. A., & Moffat, K. (2009) · Structure · doi:10.1016/j.str.2009.08.011 · Cited by 531
Self-citationStructure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499
Self-citationPhytochrome Interacting Factors: central players in phytochrome-mediated light signaling networks
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Metadata
- Authors
- Crosson, S., Rajagopal, S., & Moffat, K.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-12-11
- Volume
- 42
- Issue
- 1
- Pages
- 2-10
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2032387485
- Cited by
- 428
- References
- 9
- FWCI
- 29.85
- Type
- journal article
- Language
- en
- Open access
- closed
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