TDP-43 also acts as the transcriptional repressor and/or insulation regulator for the spatiotemporal regulation of the ACRV1 (SP-10) gene [140, 141]. TDP-43
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By changing HSPB1 and TDP-43's concentrations in vitro, the researchers found that the former ushered the latter into liquid droplets, but prevented the droplets from hardening into gels or solids. The chaperone also blocked TDP-43 from twisting into amyloid fibrils. In cells, most of the TDP-43-containing liquid droplets dissipated after the
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TDP-43 is a conserved RNA-binding protein with critical roles in splicing in the nervous system 6. TDP-43 also demonstrates tight autoregulation by binding to its transcript, triggering alternative
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TDP-43 is an RNA-binding protein that forms cytoplasmic aggregates in multiple neurodegenerative diseases. Although the loss of normal TDP-43
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In normal cells, TDP-43 is mainly present in the nucleus and plays important roles in RNA regulation, such as transcriptional regulation,
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Accordingly, TDP-43 myogranules have been shown to provide essential functions during skeletal muscle development and regeneration, both in
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Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Regulates also mRNA stability
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Cell environment shapes TDP-43 function with implications in neuronal and muscle disease. / NYGC ALS Consortium. In: Communications Biology, Vol. 5, , 314, 12.2022. Research output: Contribution to journal › Article › peer-review
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TDP-43 has diverse cellular roles in regulating RNA splicing and RNA stability as well as other gene regulatory functions 3, 4, 5. High-throughput sequencing approaches have shown that TDP-43 binds
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2020. 8. 15. · TDP-43 function, dysfunction, and aggregation. TDP-43 is a highly conserved and essential DNA/RNA binding protein belonging to the heterogenous ribonucleoprotein family
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TDP-43 binds both mRNA and DNA, thereby regulating mRNA splicing, stability and translation as well as gene transcription. Although early in vitro studies showed that TDP-43 preferentially bound RNAs via a GU dinucleotide repeat element [7], a clear consensus TDP-43 binding site in vivo has not been firmly established.
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2019. 1. 29. · Abnormal TDP-43 function culminate in impaired secretion of neurotrophin BDNF, whose restoration is sufficient to rescue major disease phenotypes caused by aberrant TDP-43 activity. Knockdown, aggregation or disease-associated mutation of TDP-43 impair intracellular sorting and activity-dependent secretion of the neurotrophin brain-derived neurotrophic factor
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Whether ALS/FTD is caused by loss of TDP-43 nuclear function (LOF) or newly gained cytoplasmic function (GOF) remains unknown. In LCDmut mice, TDP-43
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Cytosolic TDP-43 binds to numerous target mRNAs in the 3' UTR [23]. Previous studies have shown the involvement of cytosolic TDP-43 in mRNA transport and
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TDP-43 is a dimeric nuclear protein that plays a central role in RNA metabolism. In recent years, this protein has become a focal point of
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National Center for Biotechnology Information
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