Source 1review2023Journal of Molecular Biology
Toolkit/Light-Oxygen-Voltage (LOV) domain
Light-Oxygen-Voltage (LOV) domain
Also known as: LOV domain, LOV domains, LOV-sensing domain, type II light-oxygen-voltage (LOV) domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Light-Oxygen-Voltage (LOV) domain is a small blue-light-sensing protein domain used as an optogenetic input module. It binds flavin nucleotides and undergoes blue-light-induced structural rearrangements that can regulate linked effector domains, including in phototropins where LOV1 and LOV2 are coupled to a C-terminal serine/threonine kinase.
Usefulness & Problems
Why this is useful
LOV domains are useful because they are highly diverse, small blue-light sensors that have proven particularly versatile for engineering optogenetic input modules. Their use supports optical control of intracellular signaling and localization with high spatiotemporal precision, and the literature notes potential for future therapeutic strategies.
Source:
Moreover, these domains have been identified across all kingdoms of life. LOV domains are versatile photoreceptors that play critical roles in cellular signaling and environmental adaptation
Source:
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
Source:
Light–oxygen–voltage (LOV) domains, a highly diverse class of small blue light sensors, have proven to be particularly versatile for engineering optogenetic input modules.
Source:
A native threonine coordinates ordered water to tune LOV domain photocycle kinetics and osmotic stress signaling in Trichoderma reesei ENVOY.
Problem solved
LOV domains help solve the problem of how to couple a noninvasive light input to intracellular protein regulation in a genetically encoded format. The cited literature specifically supports their use for optogenetic stimulation and for controlling processes related to signaling and environmental adaptation.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
Structural CharacterizationTarget processes
localizationsignalingInput: Light
Implementation Constraints
LOV domains are flavin-binding blue-light sensors, so construct function depends on the presence of the flavin chromophore. Practical implementation commonly involves domain fusion to effector proteins; the evidence specifically notes phototropins containing two LOV domains, LOV1 and LOV2, linked to a C-terminal serine/threonine kinase domain.
The supplied evidence does not provide quantitative performance benchmarks such as dynamic range, recovery kinetics in specific constructs, or comparative data against other optogenetic modules. Independent validation of any single engineered LOV-based tool is not documented here, and therapeutic use is described only as future potential.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2review2021Journal of Biological Chemistry
Source 3primary paper2018Advanced Biosystems
Source 4primary paper2016Journal of Biological Chemistry
Source 5primary paper2013Biochemistry
Ranked Claims
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
Development of LOV-based optogenetic tools is being driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology.
The ongoing development of LOV-based optogenetic tools, driven by advances in structural biology, spectroscopy, computational methods, and synthetic biology
LOV domains are versatile photoreceptors involved in cellular signaling and environmental adaptation across kingdoms of life.
Moreover, these domains have been identified across all kingdoms of life. LOV domains are versatile photoreceptors that play critical roles in cellular signaling and environmental adaptation
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV-based optogenetic tools have potential to enable novel therapeutic strategies.
has the potential to revolutionize the study of biological systems and enable the development of novel therapeutic strategies
LOV domains use flavin nucleotides as cofactors and undergo blue-light-induced structural rearrangements that activate an effector domain.
LOV domains utilize flavin nucleotides as co-factors and undergo structural rearrangements upon exposure to blue light, which activates an effector domain that executes the final output of the photoreaction.
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Phototropins are light-activated kinases important for plant physiology and have inspired diverse optogenetic tools.
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired.
High-resolution structural information on phototropins remains challenging to obtain and is presented as important for both fundamental understanding and engineering efforts.
the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
Activation of the LOV2 domain triggers unfolding of alpha helices that communicate the light signal to the kinase domain.
activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
Recent SAXS and other biophysical studies of multidomain phototropins from Chlamydomonas and Arabidopsis support models with an extended linear domain arrangement in which the regulatory LOV2 domain contacts the kinase domain N-lobe.
Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe.
LOV domains are particularly versatile for engineering optogenetic input modules.
Light–oxygen–voltage (LOV) domains, a highly diverse class of small blue light sensors, have proven to be particularly versatile for engineering optogenetic input modules.
LOV domain-based optogenetic input modules can function via inducible allostery, protein recruitment, dimerization, or dissociation.
These can function via diverse modalities, including inducible allostery, protein recruitment, dimerization, or dissociation.
A native threonine coordinates ordered water to tune LOV domain photocycle kinetics and osmotic stress signaling in Trichoderma reesei ENVOY.
Primary photochemistry of dark-adapted YtvA is qualitatively similar to that of type I LOV domains including AsLOV2, but YtvA has a higher terminal triplet yield.
The primary photochemistry of dark-adapted YtvA is qualitatively similar to that of the type I LOV domains, including AsLOV2 from Avena sativa, but exhibits an appreciably higher (60% greater) terminal triplet yield, estimated near the maximal a6ISC value of 878%
PhiISC 78 %terminal triplet yield increase 60 %
Approval Evidence
5 sources8 linked approval claimsfirst-pass slug light-oxygen-voltage-lov-domain
The light-oxygen-voltage (LOV) domains of phototropins emerged as essential constituents of light-sensitive proteins... LOV domains are versatile photoreceptors...
Source:
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain.
Source:
Light–oxygen–voltage (LOV) domains, a highly diverse class of small blue light sensors, have proven to be particularly versatile for engineering optogenetic input modules.
Source:
Light-Oxygen-Voltage (LOV) Domain
Source:
The primary (100 fs to 10 ns) and secondary (10 ns to 100 bcs) photodynamics in the type II light-oxygen-voltage (LOV) domain
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functional scopesupports
LOV domains are versatile photoreceptors involved in cellular signaling and environmental adaptation across kingdoms of life.
Moreover, these domains have been identified across all kingdoms of life. LOV domains are versatile photoreceptors that play critical roles in cellular signaling and environmental adaptation
Source:
mechanism summarysupports
LOV domains use flavin nucleotides as cofactors and undergo blue-light-induced structural rearrangements that activate an effector domain.
LOV domains utilize flavin nucleotides as co-factors and undergo structural rearrangements upon exposure to blue light, which activates an effector domain that executes the final output of the photoreaction.
Source:
optogenetic utilitysupports
LOV domains can be used to noninvasively sense and control intracellular processes with high spatiotemporal precision, making them suitable for optogenetics.
they can noninvasively sense and control intracellular processes with high spatiotemporal precision, making them ideal candidates for use in optogenetics
Source:
domain architecturesupports
Phototropins contain two blue-light-sensing LOV domains, LOV1 and LOV2, together with a C-terminal serine/threonine kinase domain.
Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase.
Source:
functional capabilitysupports
LOV domains are particularly versatile for engineering optogenetic input modules.
Light–oxygen–voltage (LOV) domains, a highly diverse class of small blue light sensors, have proven to be particularly versatile for engineering optogenetic input modules.
Source:
mechanism modalitysupports
LOV domain-based optogenetic input modules can function via inducible allostery, protein recruitment, dimerization, or dissociation.
These can function via diverse modalities, including inducible allostery, protein recruitment, dimerization, or dissociation.
Source:
functional rolesupports
A native threonine coordinates ordered water to tune LOV domain photocycle kinetics and osmotic stress signaling in Trichoderma reesei ENVOY.
Source:
comparative photochemistrysupports
Primary photochemistry of dark-adapted YtvA is qualitatively similar to that of type I LOV domains including AsLOV2, but YtvA has a higher terminal triplet yield.
The primary photochemistry of dark-adapted YtvA is qualitatively similar to that of the type I LOV domains, including AsLOV2 from Avena sativa, but exhibits an appreciably higher (60% greater) terminal triplet yield, estimated near the maximal a6ISC value of 878%
Source:
Comparisons
Source-backed strengths
The evidence describes LOV domains as a highly diverse and versatile class of photoreceptors across kingdoms of life, supporting broad utility as engineering modules. Their activation mechanism has been studied by structural biology and spectroscopy, including primary and secondary photodynamics spanning approximately 100 fs to 100 microseconds, which supports precise temporal control.
Source:
The primary photochemistry of dark-adapted YtvA is qualitatively similar to that of the type I LOV domains, including AsLOV2 from Avena sativa, but exhibits an appreciably higher (60% greater) terminal triplet yield, estimated near the maximal a6ISC value of 878%
Ranked Citations
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