Source 1primary paper2022
Toolkit/Destruction Complex
Destruction Complex
Also known as: DC
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Destruction Complex is a Wnt signal transduction protein assembly that processes and promotes degradation of β-catenin. A 2022 study reported that nucleation of this assembly on the centrosome accelerates β-catenin degradation and changes Wnt-dependent human embryonic stem cell fate outcomes.
Usefulness & Problems
Why this is useful
This system is useful for controlling Wnt pathway output by altering where destruction complex activity is concentrated within the cell. Evidence indicates that centrosomal nucleation of the complex can tune β-catenin processing and thereby modulate downstream differentiation outcomes.
Problem solved
It addresses the problem of how to control β-catenin processing rate and Wnt signal transmission through spatial organization of the destruction complex. The cited study specifically shows that increasing the concentration of a single destruction complex kinase at the centrosome is sufficient to control β-catenin processing.
Problem links
Need conditional control of signaling activity
DerivedThe Destruction Complex is a Wnt signal transduction protein assembly that processes and promotes degradation of β-catenin. Evidence from a 2022 study indicates that nucleation of this complex on the centrosome accelerates β-catenin processing and alters Wnt-dependent cell fate outcomes.
Need conditional recombination or state switching
DerivedThe Destruction Complex is a Wnt signal transduction protein assembly that processes and promotes degradation of β-catenin. Evidence from a 2022 study indicates that nucleation of this complex on the centrosome accelerates β-catenin processing and alters Wnt-dependent cell fate outcomes.
Need inducible protein relocalization or recruitment
DerivedThe Destruction Complex is a Wnt signal transduction protein assembly that processes and promotes degradation of β-catenin. Evidence from a 2022 study indicates that nucleation of this complex on the centrosome accelerates β-catenin processing and alters Wnt-dependent cell fate outcomes.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
accelerated β-catenin processing and degradationaccelerated β-catenin processing and degradationco-localization into a reaction hubco-localization into a reaction hubnucleation of a biomolecular condensate-like assemblynucleation of a biomolecular condensate-like assemblysubcellular relocalizationsubcellular relocalizationTechniques
No technique tags yet.
Target processes
localizationrecombinationsignalingImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: actuatoroperating role: regulatorswitch architecture: multi component
Implementation is based on relocalizing destruction complex activity, including increasing the concentration of a single destruction complex kinase at the centrosome. The available evidence supports subcellular targeting and multi-component assembly control, but does not provide construct architecture, delivery modality, or expression details.
The evidence provided comes from a single 2022 study and is focused on Wnt signaling, β-catenin processing, centrosomal localization, and human embryonic stem cell differentiation. The supplied evidence does not define the full molecular composition, portability to other cell types, or performance under other signaling contexts.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug destruction-complex
Wnt signal transduction is mediated by a protein assembly called the Destruction Complex (DC)
Source:
cell fate effectsupports
Changing destruction complex kinase localization to the centrosome completely alters the fate of Wnt-driven human embryonic stem cell differentiation to mesoderm.
This simple change in localization completely alters the fate of the Wnt-driven human embryonic stem cell differentiation to mesoderm.
Source:
general mechanistic conclusionsupports
Nucleators dynamically control the activities of biomolecular condensates and may integrate cell cycle progression with Wnt signal transduction.
Our findings demonstrate the role of nucleators in dynamically controlling the activities of biomolecular condensates and suggest a tight integration between cell cycle progression and Wnt signal transduction.
Source:
localization controlsupports
Increasing the concentration of a single destruction complex kinase onto the centrosome controls β-catenin processing.
We demonstrate that simply increasing the concentration of a single DC kinase onto the centrosome controls β-catenin processing.
Source:
mechanistic functionsupports
Centrosome nucleation of the destruction complex drives efficient β-catenin processing by co-localizing destruction complex components to a single reaction hub.
we find that a function of DC nucleation by the centrosome is to drive efficient processing of β-catenin by co-localizing DC components to a single reaction hub
Source:
structural organizationsupports
The native mesoscale structure of the destruction complex is a dynamic biomolecular condensate nucleated by the centrosome.
Here we find that the native mesoscale structure is a dynamic biomolecular condensate nucleated by the centrosome.
Source:
Comparisons
Source-backed strengths
The reported strength is strong functional leverage from subcellular localization: centrosomal nucleation accelerates β-catenin degradation and completely alters Wnt-driven differentiation to mesoderm in human embryonic stem cells. The work also supports a broader mechanistic model in which nucleators dynamically regulate biomolecular condensate activity.
Compared with C-terminal iLID fusion
Destruction Complex and C-terminal iLID fusion address a similar problem space because they share localization, signaling.
Shared frame: same top-level item type; shared target processes: localization, signaling; shared mechanisms: subcellular relocalization
Compared with Opto-RhoGEFs
Destruction Complex and Opto-RhoGEFs address a similar problem space because they share localization, recombination, signaling.
Shared frame: same top-level item type; shared target processes: localization, recombination, signaling
Strengths here: looks easier to implement in practice.
Destruction Complex and single-component optogenetic tools for inducible RhoA GTPase signaling address a similar problem space because they share localization, recombination, signaling.
Shared frame: same top-level item type; shared target processes: localization, recombination, signaling
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.