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

2016. 2. 1. · TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor Hum Mol Genet. Feb 1;25(3) :534-45. doi However,

The scheme illustrates that TDP-43 functions normally as dimer or oligomer conformers in the nuclear compartment. However, upon translocation to the cytoplasm, truncation of TDP-43 promotes aggregation (gain-of-function).

TDP-43 is an RNA binding protein of 43 kDa that belongs to the hnRNP family and plays numerous roles in mRNA metabolism such as transcription, 

TDP-43 is an essential RNA-binding protein that assembles into protein inclusions in >95% of cases of amyotrophic lateral sclerosis (ALS). A partially helical region in the predominantly disordered C-terminal domain harbors several mutations associated with ALS and is important for TDP-43 function and liquid-liquid phase separation.

TDP-43 May be Increased in ALS Leading to Neurotoxicity from Both Gain and Loss of Functions · by Z Xu · · Cited by 15 —

Most importantly, the expression of hnRNP A1/A2 and PTB/nPTB is significantly altered in patients with frontotemporal dementia with TDP-43-positive inclusions (FTLD-TDP), indicating that perturbations in RNA metabolism and processing in FTLD-TDP are not exclusively driven by a loss of TDP-43 function.

2021. 10. 25. · Dendritic spine loss induced by TDP-43 knockdown is rescued by wild-type TDP-43, but not ALS/FTLD-associated mutants, suggesting a common TDP-43 functional deficiency

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

TDP-43 aggregation and redistribution have been recognised as a hallmark of amyotrophic lateral sclerosis, frontotemporal dementia and other neurological disorders. While TDP-43 has been studied extensively in neuronal tissues, TDP-43 inclusions have also been described in the muscle of inclusion body myositis patients, highlighting the need to understand the role of TDP-43 beyond the central

Loss of TDP-43 function underlies hippocampal and cortical synaptic deficits in TDP-43 proteinopathies Loss of TDP-43 function underlies hippocampal and cortical synaptic deficits in TDP-43 proteinopathies Mol Psychiatry. Oct 25. doi: 10.1038/s41380-021-01346-. Online ahead of print. Authors

TDP-43 is a protein that regulates gene expression. TDP-43 aggregation and depletion from cell nucleus are found in ALS. Therefore, TDP-43 may 

An acetylation switch controls TDP-43 function and aggregation propensity TDP-43 pathology is a disease hallmark that characterizes amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP). Although a critical role for TDP-43 as an RNA-binding protein has emerged, the regulation of TDP-43 function is poorly understood.

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Functions of TDP-43. TDP-43 performs several mRNA-related processes in the nucleus, such as transcription, splicing, maintaining RNA stability as well as miRNA and lncRNA processing. It is predominantly a nuclear protein but also shuttles between the nucleus and the cytoplasm.

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 

TDP-43 is a protein that regulates gene expression. TDP-43 aggregation and depletion from cell nucleus are found in ALS. Therefore, TDP-43 may cause neurodegeneration by generating toxicity from its aggregation or by a loss of its function. Our experiments test the consequence of a partial loss of TDP-43 function in mice.

2014. 2. 1. · TDP-43 is normally expressed in the nucleus of neurons where its most important function is to regulate RNA processing, including mRNA splicing, mainly by binding to UG-rich intronic regions 11, 12.However, in the ALS–FTD patients, TDP-43-positive inclusions are typically found in the neuronal cytoplasm and accompanied by a loss of the normal nuclear expression

In normal cells, TDP-43 is mainly present in the nucleus and plays important roles in RNA regulation, such as transcriptional regulation, 

Alterations in TDP-43 are commonly found in patients suffering from amyotrophic lateral sclerosis (ALS) and the genetic suppression of the conserved homologue in Drosophila (TBPH) provokes alterations in the functional organization of motoneuron

Phosphorylated TDP-43 potentiates a number of neurotoxic effects including reduced liquid–liquid phase separation dynamicity, changes in 

16 hours ago · TDP-43 protein is 96 percent identical between human and mice, and more than a dozen knockout and transgenic lines of wild-type and mutant TDP-43 have been created. Most

Transactive response DNA binding protein 43 (TDP-43) is a DNA/RNA binding protein involved in transcriptional regulation and RNA processing. It is linked.

TDP-43 deficiency leads to decreased dynactin 1 expression, blocking autophagic flux; it also reduces mTORC1 activity, leading to increased autophagy and lysosome gene expression via TFEB. Abnormal regulation of autophagy contributes to TDP-43-associated neurotoxicity. TDP-43 is required for raptor mRNA stability and thus for mTORC1 activity.

TDP-43 physiological functions and pathobiology. The protein structure of TDP-43 and its involvement in ALS/. FTLD diseases have already been described in 

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