Source 1primary paper2021ACS Synthetic Biology
Toolkit/fusion proteins with large N-terminal anchors
fusion proteins with large N-terminal anchors
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Fusion proteins with large N-terminal anchors are an anchor-design variant for the light-inducible iLID recruitment system. In this configuration, the modified anchor supports light-controlled recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane, to improve control of protein localization and signaling outputs.
Usefulness & Problems
Why this is useful
This design is useful for experiments requiring tighter optogenetic control of subcellular protein localization. The cited study frames these anchor variants as tools for greater control across diverse cell biological applications and for selective recruitment to defined subcellular regions.
Source:
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Source:
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
Source:
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
Problem solved
This tool addresses the problem of achieving selective light-inducible recruitment of proteins to precise subcellular locations. The available evidence specifically supports improved control over localization at sites such as micron-scale regions of the plasma membrane.
Source:
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
HeterodimerizationTechniques
No technique tags yet.
Target processes
localizationsignalingInput: Light
Implementation Constraints
This tool is implemented within the iLID light-inducible recruitment system and uses fusion proteins with large N-terminal anchors. The provided evidence does not specify construct architecture beyond the N-terminal anchor feature, nor does it state illumination wavelength, expression context, or cofactor requirements.
The supplied evidence is limited to a single source and provides little direct mechanistic or performance detail for the large N-terminal anchor configuration itself. No explicit data are provided here on kinetics, dynamic range, reversibility, cell-type generality, or comparisons against other anchor architectures.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug fusion-proteins-with-large-n-terminal-anchors
fusion proteins with large N-terminal anchors
Source:
application scopesupports
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Source:
comparative performancesupports
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Source:
mechanistic effectsupports
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Source:
Comparisons
Source-backed strengths
The available evidence supports selective recruitment of components to subcellular locations, including micron-scale plasma membrane regions. The current summary further attributes improved recruitment performance to large N-terminal anchors through stronger local recruitment, slower diffusion of recruited components, and improved spatial control, but the provided extraction text does not include quantitative benchmarking.
Source:
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Ranked Citations
- 1.