Source 1primary paper2014Proceedings of the National Academy of Sciences
Toolkit/light-oxygen-voltage (LOV) sensor domain
light-oxygen-voltage (LOV) sensor domain
Also known as: LOV sensor domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The light-oxygen-voltage (LOV) sensor domain is a light-responsive regulatory protein domain characterized in the monomeric histidine kinase EL346. Structural evidence indicates that it binds one side of the DHpL domain to control kinase output, prevent dimerization, and release the catalytic apparatus from an inhibited conformation upon photoactivation.
Usefulness & Problems
Why this is useful
This domain is useful as a genetically encoded light input module for regulating histidine kinase signaling through intramolecular control of catalytic state. The available evidence specifically supports its ability to couple light sensing to changes in DHpL/CA domain organization and kinase regulation in EL346.
Problem solved
It addresses the problem of how a photosensory domain can regulate a monomeric histidine kinase without relying on constitutive dimerization. In EL346, the LOV domain provides a structural mechanism for maintaining dark-state inhibition and relieving that inhibition after light activation.
Problem links
Need conditional control of signaling activity
DerivedThe light-oxygen-voltage (LOV) sensor domain is a light-responsive protein domain characterized here in the monomeric histidine kinase EL346. Structural evidence indicates that it regulates kinase output by binding one side of the DHpL domain, preventing dimerization and controlling the inhibited versus activated state of the catalytic apparatus.
Need precise spatiotemporal control with light input
DerivedThe light-oxygen-voltage (LOV) sensor domain is a light-responsive protein domain characterized here in the monomeric histidine kinase EL346. Structural evidence indicates that it regulates kinase output by binding one side of the DHpL domain, preventing dimerization and controlling the inhibited versus activated state of the catalytic apparatus.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
Heterodimerizationinhibition of dimerizationinhibition of dimerizationinterdomain interaction weakening upon photoactivationinterdomain interaction weakening upon photoactivationlight-dependent allosteric switchinglight-dependent allosteric switchingTechniques
No technique tags yet.
Target processes
signalingInput: 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: sensorswitch architecture: multi componentswitch architecture: recruitmentswitch architecture: uncaging
The supported implementation context is the full-length monomeric histidine kinase EL346, where the LOV domain acts through physical interaction with the DHpL domain and influences the DHpL/CA interface. The supplied evidence does not provide construct design rules, cofactor requirements, expression conditions, or delivery guidance.
The evidence appears to come from a single structural study in one protein context, EL346. Quantitative performance metrics, spectral parameters, transferability to other proteins, and independent replication are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug light-oxygen-voltage-lov-sensor-domain
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization
Source:
mechanism of regulationsupports
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
Source:
mechanistic modelsupports
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
Source:
Comparisons
Source-backed strengths
Structural analysis of full-length EL346 provides a concrete mechanistic model linking the LOV domain to kinase regulation. The evidence supports multiple connected functions: prevention of dimerization, stabilization of an inhibited dark-state arrangement, and photoactivation-associated release of the CA domain from inhibition.
Compared with EL346
light-oxygen-voltage (LOV) sensor domain and EL346 address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization, light-dependent allosteric switching; same primary input modality: light
Compared with light-oxygen-voltage sensing (LOV) domain
light-oxygen-voltage (LOV) sensor domain and light-oxygen-voltage sensing (LOV) domain address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Compared with optogenetic RGS2
light-oxygen-voltage (LOV) sensor domain and optogenetic RGS2 address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Ranked Citations
- 1.