Source 1primary paper2014Proceedings of the National Academy of Sciences
Toolkit/LOV2 domain from Avena sativa
LOV2 domain from Avena sativa
Also known as: light-oxygen-voltage 2 (LOV2) domain, light/oxygen/voltage-sensitive domain 2, LOV2
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Avena sativa LOV2 domain is a blue-light-sensing photosensory domain used as a photoswitchable scaffold for engineered control of protein interactions. In the iLID design, the bacterial SsrA peptide is embedded in the LOV2 C-terminal helix so that blue light triggers helix undocking and enables binding to SspB.
Usefulness & Problems
Why this is useful
This domain is useful as a genetically encoded light input module for reversible optical control of protein localization and signaling. Source evidence specifically supports its use in iLID to drive light-mediated subcellular localization in mammalian cells and reversible control of small GTPase signaling.
Source:
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
Problem solved
It addresses the problem of making a protein-protein interaction conditional on light rather than constitutive. In the cited design, LOV2 cages the SsrA peptide in the dark and releases access upon blue-light activation, allowing temporal control of SspB recruitment.
Source:
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
Problem links
Need conditional recombination or state switching
DerivedThe Avena sativa LOV2 domain is a blue-light-sensing protein domain used as a photoswitchable scaffold for engineered control of protein interactions. In the cited iLID design, embedding the bacterial SsrA peptide in the LOV2 C-terminal helix enables light-dependent binding to SspB through a preserved LOV2 photoreaction and helix undocking.
Need precise spatiotemporal control with light input
DerivedThe Avena sativa LOV2 domain is a blue-light-sensing protein domain used as a photoswitchable scaffold for engineered control of protein interactions. In the cited iLID design, embedding the bacterial SsrA peptide in the LOV2 C-terminal helix enables light-dependent binding to SspB through a preserved LOV2 photoreaction and helix undocking.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational uncagingconformational uncagingConformational UncagingHeterodimerizationHeterodimerizationHeterodimerizationlight-induced helix undockinglight-induced helix undockingTechniques
Structural CharacterizationTarget processes
recombinationInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitmentswitch architecture: uncaging
The documented construct design embeds the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain. Practical use in the cited application involves pairing this engineered LOV2 module with the SspB binding partner and activating it with blue light in mammalian cell culture.
The supplied evidence is limited to the iLID-style SsrA/SspB implementation and does not provide quantitative kinetics, dynamic range, wavelength dependence beyond blue light, or performance across diverse organisms. Independent replication is not established from the provided sources.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2017FEBS Journal
Ranked Claims
The LOV2 photoreaction is preserved in the PiL[D24] chimera.
The LOV2 photoreaction is preserved in the PiL[D24] chimera
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
Approval Evidence
2 sources4 linked approval claimsfirst-pass slug lov2-domain-from-avena-sativa
the light-sensing LOV2 domain from Avena Sativa
Source:
we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa
Source:
mechanismsupports
The LOV2 photoreaction is preserved in the PiL[D24] chimera.
The LOV2 photoreaction is preserved in the PiL[D24] chimera
Source:
engineering strategysupports
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
Source:
mechanismsupports
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
Source:
structural mechanismsupports
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
Source:
Comparisons
Source-backed strengths
The cited work reports that the LOV2 photoreaction is preserved after engineering of the chimera, indicating that the photosensory function tolerates peptide insertion in this context. The system was functionally demonstrated in mammalian cell culture through light-mediated subcellular localization and reversible control of small GTPase signaling.
Source:
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
Source:
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Source:
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
Compared with Avena sativa phototropin-1 LOV2 domain
LOV2 domain from Avena sativa and Avena sativa phototropin-1 LOV2 domain address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Compared with optogenetic RGS2
LOV2 domain from Avena sativa and optogenetic RGS2 address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with SspB
LOV2 domain from Avena sativa and SspB address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: conformational uncaging, conformational_uncaging, heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated.
Ranked Citations
- 1.