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Reduction of RAD23A extends lifespan and mitigates pathology in TDP-43 mice

Xueshui, G. n.; Prajapati, R. n.; Chun, J. n.; Byun, I. n.; Gebis, K. K.; Wang, Y.-Z. n.; Ling, K. n.; Dalton, C. n.; Blair, J. A.; Hamidianjahromi, A. n.; Bachmann, G. n.; Rigo, F. n.; Jafar-nejad, P. n.; Savas, J. n.; Lee, M. J.; Sreedharan,, J. n.; Kalb, R.

2024-09-14 neuroscience
10.1101/2024.09.10.612226 bioRxiv
Show abstract

Protein misfolding and aggregation are cardinal features of neurodegenerative disease (NDD) and they contribute to pathophysiology by both loss-of-function (LOF) and gain-of-function (GOF) mechanisms. This is well exemplified by TDP-43 which aggregates and mislocalizes in several NDDs. The depletion of nuclear TDP-43 leads to reduction in its normal function in RNA metabolism and the cytoplasmic accumulation of TDP-43 leads to aberrant protein homeostasis. A modifier screen found that loss of rad23 suppressed TDP-43 pathology in invertebrate and tissue culture models. Here we show in a mouse model of TDP-43 pathology that genetic or antisense oligonucleotide (ASO)-mediated reduction in rad23a confers benefits on survival and behavior, histological hallmarks of disease and reduction of mislocalized and aggregated TDP-43. This results in improved function of the ubiquitin-proteasome system (UPS) and correction of transcriptomic alterations evoked by pathologic TDP-43. RAD23A-dependent remodeling of the insoluble proteome appears to be a key event driving pathology in this model. As TDP-43 pathology is prevalent in both familial and sporadic NDD, targeting RAD23A may have therapeutic potential.

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