Source 1primary paper2012Proteins Structure Function and Bioinformatics
Toolkit/AsLOV2-Jα-Rac1
AsLOV2-Jα-Rac1
Also known as: AsLOV2-Jα-Rac1-photoenzyme
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
AsLOV2-Jα-Rac1 is an artificial fusion protein that connects the Avena sativa AsLOV2-Jα photosensor to the Rac1 GTPase to create a light-responsive signaling switch. Light-triggered structural changes in the LOV2 module disrupt steric inhibition of Rac1 and permit binding of the effector protein PAK1.
Usefulness & Problems
Why this is useful
This tool is useful for optical control of Rac1-dependent signaling with a genetically encoded fusion architecture. Source literature reports its use to control motility of HeLa cancer cells upon light stimulation.
Source:
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Problem solved
AsLOV2-Jα-Rac1 addresses the problem of externally controlling Rac1 activity in living cells with light rather than constitutive or non-optical perturbation. The cited work specifically links this capability to control of early-stage signaling associated with cell motility.
Source:
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
fmn-cys450 photoadduct formationhydrogen-bond rearrangement involving fmn and gln513jα-helix disruptionlight-dependent release of steric inhibition enabling pak1 bindinglight-induced allosteric switchingβ-sheet tightening and torsional stress transmissionTechniques
Computational DesignTarget processes
signalingInput: Light
Implementation Constraints
The construct is described as a fusion of the Avena sativa AsLOV2-Jα photosensor with Rac1-GTPase. The mechanistic model specifically involves FMN and Cys450 within the LOV2 module, but the supplied evidence does not provide construct architecture details, expression conditions, or delivery methods.
The supplied evidence is limited to one cited study and emphasizes mechanistic simulation plus a reported HeLa cell motility application. Quantitative performance characteristics, spectral parameters, dynamic range, reversibility, and validation across multiple cell types or independent groups are not provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
successMammalian Cell Lineapplication demoHeLa
Inferred from claim c1 during normalization. The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus. Derived from claim c1. Quoted text: This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
Supporting Sources
Ranked Claims
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
Approval Evidence
1 source4 linked approval claimsfirst-pass slug aslov2-j-rac1
designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1)
Source:
application capabilitysupports
The artificial fusion protein AsLOV2-Jα-Rac1 was used to control motility of HeLa cancer cells upon light stimulus.
This has recently been impressively demonstrated by designing a novel artificial fusion protein, connecting the AsLOV2-Jα-photosensor from Avena sativa with the Rac1-GTPase (AsLOV2-Jα-Rac1), and by using it, to control the motility of cancer cells from the HeLa-line.
Source:
mechanistic pathwaysupports
Computer simulations indicate that after Cys450-FMN adduct formation in AsLOV2-Jα-Rac1, an H-bond between FMN-C4 oxygen and Gln513 breaks and Gln513 reorients.
Here, we show through computer simulations of the AsLOV2-Jα-Rac1-photoenzyme that the early processes after formation of the Cys450-FMN-adduct involve the breakage of a H-bond between the carbonyl oxygen FMN-C4O and the amino group of Gln513, followed by a rotational reorientation of its sidechain.
Source:
mechanistic pathwaysupports
Disruption of the Jα-helix triggers detachment of the AsLOV2-Jα photosensor from Rac1-GTPase, enabling activation of Rac1 via binding of the effector protein PAK1.
Finally, this process triggers the detachment of the AsLOV2-Jα-photosensor from the Rac1-GTPase, ultimately enabling the activation of Rac1 via binding of the effector protein PAK1.
Source:
mechanistic pathwaysupports
The initial photochemical event is followed by β-sheet tightening and torsional stress transmission along the Iβ-sheet, leading to disruption of the Jα-helix from the N-terminal end.
This initial event is followed by successive events including β-sheet tightening and transmission of torsional stress along the Iβ-sheet, which leads to the disruption of the Jα-helix from the N-terminal end.
Source:
Comparisons
Source-backed strengths
The tool couples a defined plant LOV2 photosensor to Rac1 in a single artificial fusion protein, providing a direct route from light input to GTPase regulation. Mechanistic analysis from computer simulations supports a detailed pathway from Cys450-FMN photoadduct formation through β-sheet tightening and Jα-helix disruption to PAK1-accessible Rac1 activation.
Ranked Citations
- 1.