Source 1primary paper2019
Toolkit/GLIMPSe
GLIMPSe
Also known as: generalizable light modulated protein stabilization system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
GLIMPSe is a generalizable light-modulated protein stabilization system for optogenetic control of intracellular protein abundance independent of the target protein’s intrinsic function. It is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Usefulness & Problems
Why this is useful
GLIMPSe is useful because it enables target-independent optogenetic control of protein activities by regulating intracellular protein level rather than relying on target-specific photoactivatable protein engineering. The source literature states that this design minimizes systematic variation embedded within different photoactivatable proteins.
Source:
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Source:
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
Source:
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
Problem solved
GLIMPSe addresses the problem of controlling protein activity with light when direct photoengineering of each target protein is difficult or introduces target-specific variability. The reported solution is post-translational, light-mediated stabilization of proteins in live cells independent of the target protein’s native functionality.
Source:
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Source:
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
Problem links
Need conditional control of signaling activity
DerivedGLIMPSe is a generalizable light-modulated protein stabilization system for optogenetic control of intracellular protein abundance independent of the target protein’s intrinsic function. It is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Need precise spatiotemporal control with light input
DerivedGLIMPSe is a generalizable light-modulated protein stabilization system for optogenetic control of intracellular protein abundance independent of the target protein’s intrinsic function. It is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Need tighter control over protein production
DerivedGLIMPSe is a generalizable light-modulated protein stabilization system for optogenetic control of intracellular protein abundance independent of the target protein’s intrinsic function. It is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
light-induced protein stabilizationpost-translational control of protein abundanceTranslation ControlTechniques
No technique tags yet.
Target processes
signalingtranslationInput: 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 component
The available evidence supports that GLIMPSe is a multi-component, light-responsive system operating through post-translational protein stabilization in live cells. The supplied material does not specify construct architecture, chromophore requirements, host systems, delivery modality, or exact illumination parameters.
The supplied evidence does not provide quantitative performance metrics, kinetic parameters, dynamic range, reversibility, or wavelength-specific implementation details. Validation described here is limited to the originating study and a small number of named examples in the ERK pathway.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
time to light-induced protein stabilization 1 minute
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
Approval Evidence
1 source5 linked approval claimsfirst-pass slug glimpse
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
Source:
advantagesupports
GLIMPSe enables target-independent optogenetic control of protein activities and minimizes systematic variation embedded within different photoactivatable proteins.
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
Source:
application scopesupports
GLIMPSe is presented as a method for light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Overall, GLIMPSe promises to achieve light-mediated post-translational stabilization of a wide array of target proteins in live cells.
Source:
application scopesupports
GLIMPSe was applied to control MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
We applied GLIMPSe to control two distinct classes of proteins: mitogen-activated protein kinase phosphatase 3 (MKP3), a negative regulator of the extracellular signal-regulated kinase (ERK) pathway, as well as a constitutively active form of MEK (CA MEK), a positive regulator of the same pathway.
Source:
kineticssupports
Light-induced protein stabilization with GLIMPSe can be achieved within 1 minute of blue light stimulation.
Kinetics study showed that light-induced protein stabilization could be achieved within 1 minute of blue light stimulation.
Source:
tool capabilitysupports
GLIMPSe controls intracellular protein level independent of target protein functionality.
we developed a generalizable light modulated protein stabilization system (GLIMPSe) to control intracellular protein level independent of its functionality
Source:
Comparisons
Source-backed strengths
The reported strength of GLIMPSe is its generalizability across targets, with source claims describing a wide application scope and target-independent control. It was applied to MKP3 and constitutively active MEK, representing two distinct classes of proteins in the ERK pathway.
Source:
GLIMPSe enables target-independent optogenetic control of protein activities and therefore minimizes the systematic variation embedded within different photoactivatable proteins.
Compared with cLIPS1
GLIMPSe and cLIPS1 address a similar problem space because they share translation.
Shared frame: same top-level item type; shared target processes: translation; shared mechanisms: translation_control; same primary input modality: light
Compared with fifth-generation CAR-T cells
GLIMPSe and fifth-generation CAR-T cells address a similar problem space because they share signaling, translation.
Shared frame: same top-level item type; shared target processes: signaling, translation; shared mechanisms: translation_control
Relative tradeoffs: looks easier to implement in practice.
Compared with optogenetic systems adapted to regulate gene expression
GLIMPSe and optogenetic systems adapted to regulate gene expression address a similar problem space because they share translation.
Shared frame: same top-level item type; shared target processes: translation; shared mechanisms: translation_control; same primary input modality: light
Ranked Citations
- 1.