Optogenetic Tdp-43
Optogenetic Tdp-43 - Related Videos
07:14
Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae
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2022
We describe a protocol to induce phase transition of TAR DNA-binding protein 43 (TDP-43) by light in the spinal motor neurons using zebrafish as a model.
13:31
Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
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Cited by 17 •
2015
Using atomic force microscopy in combination with biopanning technology we created a negative and positive biopanning system to acquire antibodies against disease-specific protein variants present in any biological material, even at low concentrations. We were successful in obtaining antibodies to TDP-43 protein variants involved in Amyotrophic Lateral Sclerosis.
07:07
Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
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Cited by 3 •
2021
Glucose uptake is increased in Drosophila motor neurons affected by TAR DNA binding protein (TDP-43) proteinopathy, as indicated by a FRET-based, genetically encoded glucose sensor.
04:38
Protein Phase Separation Assay: An Optogenetic Method for Mutant RNA-Binding Protein Phase Separation in Spinal Motor Neurons of Zebrafish Larvae
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2025
In this video, we describe a phase separation assay, wherein intracellular proteins comprising intrinsically disordered regions fused to a photosensitive oligomerization domain are induced via blue-light exposure to self-associate into membrane-less liquid-like condensates.
06:06
Optogenetic Functional MRI
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Cited by 15 •
2016
This protocol describes the steps and data analysis required to successfully perform optogenetic functional magnetic resonance imaging (ofMRI). ofMRI is a novel technique that combines high-field fMRI readout with optogenetic stimulation, allowing for cell type-specific mapping of functional neural circuits and their dynamics across the whole living brain.
FAQs
The attached photoreceptor converts illumination into a controllable change in TDP-43 assembly. Blue light typically promotes rapid clustering or condensation, enabling researchers to compare cellular states before and after activation. This temporal control helps separate light-induced changes in TDP-43 organization from later consequences for localization, RNA regulation, or cellular toxicity.
Monitoring localization shows where TDP-43 resides within living cells, whereas examining assembly reveals whether it forms clusters or condensed structures. Considering both readouts helps researchers determine whether an observed change reflects redistribution, altered condensation, or both. That distinction is important when connecting TDP-43 organization with RNA-related effects and disease-associated cellular behavior.
TDP-43 phase behavior describes how the protein changes between more dispersed and condensed states, while stress-granule interactions address how those states relate to cellular stress structures. Light-controlled clustering provides a way to examine these relationships in living cells. The resulting observations can clarify whether altered assembly accompanies changes in RNA regulation or toxicity.
Light control provides a defined experimental trigger for changing TDP-43 assembly, rather than relying only on changes that arise without deliberate activation. Researchers can then observe the sequence linking condensation with localization, RNA regulation, stress-granule interactions, or toxicity. This precision supports more focused tests of how TDP-43 behavior contributes to neurodegenerative disease mechanisms.
A typical workflow uses living cells containing TDP-43 fused to a light-sensitive photoreceptor, followed by illumination, usually with blue light. Researchers then observe the resulting clustering or condensation and assess associated changes in localization or assembly. The approach can be extended to examine RNA regulation, stress-granule interactions, and toxicity within the same experimental framework.
Illumination is the key controlled condition, with blue light typically used to promote TDP-43 clustering or condensation. Observations focus on how rapidly assembly appears and how cellular localization changes afterward. Researchers can relate these visual and organizational outcomes to RNA regulation, stress-granule interactions, or toxicity, depending on the biological question being tested.
The system provides a controlled way to examine TDP-43 behavior in models relevant to amyotrophic lateral sclerosis and frontotemporal dementia. By inducing and observing condensation, researchers can investigate how altered assembly relates to disease-associated mechanisms, including RNA regulation and cellular toxicity. These experiments help connect molecular behavior with broader neurodegenerative disease context.
Because illumination supplies a precise trigger for changing TDP-43 assembly, researchers can use the system to test how an intervention affects downstream or associated outcomes. Comparisons may focus on clustering, localization, RNA regulation, stress-granule interactions, or toxicity after controlled activation. This creates a structured framework for evaluating whether a candidate intervention changes disease-relevant TDP-43 behavior.