Source 1primary paper2022
Toolkit/biofunctional nanodot arrays
biofunctional nanodot arrays
Also known as: bNDAs
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Biofunctional nanodot arrays (bNDAs) are nanoscale surface-patterned delivery harnesses designed to spatially control dimerization and clustering of cell-surface receptors. In live cells, they were used to capture extracellularly GFP-tagged Lrp6 and drive assembly of active Wnt signalosomes at the plasma membrane.
Usefulness & Problems
Why this is useful
bNDAs are useful for imposing nanoscale spatial organization on membrane receptors in living cells and for experimentally triggering localized signaling complex assembly. In the reported application, they enabled analysis of Wnt signalosome formation and provided evidence for synergistic co-condensation associated with signaling amplification.
Source:
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Source:
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
Source:
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Problem solved
bNDAs address the problem of how to control receptor dimerization and clustering at the plasma membrane with nanoscale spatial precision in live-cell experiments. They were specifically applied to organize Lrp6 at the cell surface and probe how spatially constrained assembly contributes to Wnt signalodroplet formation.
Source:
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Source:
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Problem links
This item directly concerns nanoscale spatial patterning via nanodot arrays, which is closer to the gap's need for assembling diverse molecular components without relying on conventional chip-fab workflows. It plausibly offers a more reconfigurable surface-patterning strategy for small-scale molecular organization.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A delivery strategy grouped with the mechanism branch because it determines how a system is instantiated and deployed in context.
Mechanisms
HeterodimerizationHeterodimerizationHeterodimerizationliquid-liquid phase separationliquid-liquid phase separationreceptor clusteringreceptor clusteringTechniques
No technique tags yet.
Target processes
localizationsignalingInput: Chemical
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: externally suppliedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: deliveryswitch architecture: multi componentswitch architecture: recruitment
The reported implementation relied on nanoscale surface patterning and affinity-based capture of extracellularly GFP-tagged Lrp6 at the plasma membrane of live cells. The evidence supports use as a surface-presented harness for receptor organization, but does not specify fabrication chemistry, substrate composition, or delivery conditions.
The supplied evidence describes a single reported application centered on extracellularly GFP-tagged Lrp6 and Wnt signaling, so generality across receptors, cell types, and signaling systems is not established here. Practical performance metrics such as throughput, fabrication robustness, and compatibility with non-tagged endogenous targets are not provided in the evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
spot diameter 300 nm
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
Approval Evidence
1 source7 linked approval claimsfirst-pass slug biofunctional-nanodot-arrays
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
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application demosupports
Biofunctional nanodot arrays enabled spatially controlled assembly of active Wnt signalosomes at the plasma membrane of live cells by capturing Lrp6 via an extracellular GFP tag.
We achieved spatially controlled assembly of active Wnt signalosomes at the nanoscale in the plasma membrane of live cells by capturing the co-receptor Lrp6 into bNDAs via an extracellular GFP tag.
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functional implicationsupports
The observations indicate synergistic effects of LLPS for Wnt signaling amplification.
pinpointing the synergistic effects of LLPS for Wnt signaling amplification.
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mechanistic inferencesupports
Density variation and high effector-protein dynamics support a highly cooperative LLPS-driven assembly of Wnt signalodroplets at the plasma membrane.
Density variation and the high dynamics of effector proteins uncover highly cooperative liquid-liquid phase separation (LLPS)-driven assembly of Wnt “signalodroplets” at the plasma membrane
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physical characteristicsupports
The reported biofunctional nanodot arrays had spot diameters of approximately 300 nm.
High-contrast bNDAs with spot diameters of ∼300 nm were obtained by capillary nanostamping of BSA bioconjugates
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recruitment observationsupports
Frizzled-8, Axin-1, and Disheveled-2 were co-recruited into Lrp6 nanodots in the absence of ligand.
Strikingly, we observed co-recruitment of co-receptor Frizzled-8 as well as the cytosolic scaffold proteins Axin-1 and Disheveled-2 into Lrp6 nanodots in the absence of ligand.
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tool developmentsupports
Biofunctional nanodot arrays were developed to spatially control dimerization and clustering of cell surface receptors at the nanoscale.
Here, we have developed biofunctional nanodot arrays (bNDAs) to spatially control dimerization and clustering of cell surface receptors at nanoscale.
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use potentialsupports
Biofunctional nanodot arrays have potential for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
These insights highlight the potential of bNDAs for systematically interrogating nanoscale signaling platforms and condensation at the plasma membrane of live cells.
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Comparisons
Source-backed strengths
The tool was demonstrated in live cells and supported spatially controlled assembly of active Wnt signalosomes at the plasma membrane. The study further reported density-dependent behavior and high effector-protein dynamics consistent with a highly cooperative liquid-liquid phase separation-driven assembly process.
Compared with CIB1
biofunctional nanodot arrays and CIB1 address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; shared mechanisms: heterodimerization; same primary input modality: chemical
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with Opto-RhoGEFs
biofunctional nanodot arrays and Opto-RhoGEFs address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
biofunctional nanodot arrays and single-component optogenetic tools for inducible RhoA GTPase signaling address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.