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Fig. 8

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ZDB-FIG-200306-111

Publication

Asakawa et al., 2020 - Optogenetic modulation of TDP-43 oligomerization accelerates ALS-related pathologies in the spinal motor neurons

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Fig. 8

Sequentially regulated illumination-triggered TDP-43 knot and aggregate formation.

In physiological conditions, TDP-43 forms oligomers via its N-terminus and is primarily localized in the nucleus. Spinal motor neurons keep the cytoplasmic concentration of TDP-43 oligomers at a low level to prevent them from turning into toxic irreversible oligomers mediated by the C-terminus IDRs (toxic “knots”), which possess competence for developing into pathological TDP-43 aggregates, a hallmark of ALS. CRY2olig-driven opTDP-43 oligomerization promotes pathological change of the motor neurons, such as axon retraction associated with myofiber denervation, prior to accumulation of distinct cytoplasmic aggregates. Whether CRY2olig-diriven opTDP-43 aggregates are toxic to motor neurons and whether CRY2olig-diriven aggregates eventually deplete endogenous nuclear TDP-43 pools are unknown.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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