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Human TARDBP Protein expressed in HEK-293 Cells - ABIN2733240
Yang, Lin, Robertson, Wang: Dual vulnerability of TDP-43 to calpain and caspase-3 proteolysis after neurotoxic conditions and traumatic brain injury. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2014
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more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS (show FUS Proteins) than in FTLD-tau
study found a high frequency of the TARDBP p.M337 V mutation in familial amyotrophic lateral sclerosis (ALS) in south-eastern China; the TARDBP-linked ALS patients showed a benign disease course and prolonged survival
describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 (show SOD1 Proteins) and TARDP genes
Study indicates that there are at least two common patterns of TDP-43 and tau protein misfolding in human brain aging. In patients lacking substantial Alzheimer's disease pathology, cerebral age-related TDP-43 with sclerosis (CARTS) cases tend to have tau neurofibrillary tangles in the hippocampal dentate granule neurons, providing a potential proxy indicator of CARTS.
Dep (show FUS Proteins)letion of (show TAF15 Proteins)TAF15, FUS and TDP-43 in human-induced pluripotent stem cell-derived motor neurons affects different genes.
TDP-43 mislocalisation into axons precedes cell death in cortical neurons, and that cytoskeletal structure and function is impaired by expression of either TDP-43 wild-type or mutant constructs in vitro.
TDP-43 impairs the induction of multiple key stress genes required to protect from disease by reducing the recruitment of the chromatin remodeler Chd1 to chromatin.
The mutation of TARDBP caused amyotrophic lateral sclerosis
Cytoplasmic TDP-43 mislocalization and aggregation is a pathological hallmark of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 is an RNA-binding protein (show PTBP1 Proteins) with a prion (show PRNP Proteins)-like domain that promotes TDP-43 misfolding. [review]
SOD1 mutations were present in 20% of familial amyotrophic lateral sclerosis (ALS) patients and 1.9% of sporadic ALS patients, while FUS mutations were responsible for 13.3% of familial ALS cases, and TARDBP mutations were rare in either familial or sporadic ALS cases.
FUS (show FUS Proteins) and TAF15 (show TAF15 Proteins) exhibit similar global RNA interaction profiles in vivo, but affect a strikingly small subset of common genes. Unexpectedly, TAF15 (show TAF15 Proteins) influences a small fraction of amyotrophic lateral sclerosis events compared with TDP-43 and FUS (show FUS Proteins) in the mouse CNS.
Increased excitatory synaptic inputs and dendritic spine densities is associated with TDP-43(Q331K) mutation resulting in amyotrophic lateral sclerosis.
Given the close association of stress granules and TDP-43, we wondered whether internalisation of SOD1 (show SOD1 Proteins) aggregates stimulated TDP-43 cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 (show SOD1 Proteins) aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 to the cytoplasm where it was still accumulated after 48 h.
The mutated TDP-43 has a significant pathological effect at the dendritic spine that is associated with attenuated neural transmission.
Studied expression and localization of TAR DNA-binding protein 43 (TDP-43) in mouse seminiferous epithelium. Found TDP-43 is expressed by both germ cells and Sertoli cells and appears to have a role in specific stages of spermatogenesis.
TDP-43 overexpression decreases amyloid-Beta plaque deposition while increasing abnormal tau aggregation.
results suggest that regulation of the U6 snRNA expression level by TDP-43 is a key factor in the increase in cell death upon TDP-43 loss-of-function
this study shows that HSF1 (show HSF1 Proteins) overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70 (show HSP70 Proteins), rather than enhancing autophagy
Acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1 (show HSF1 Proteins)-dependent chaperone mechanism that disaggregates the protein.
These studies showed that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation.
Data indicate a method for site-directed single nucleotide editing in two disease-related genes, DNA binding protein (show CNBP Proteins) tardbp and RNA binding protein fus (show FUS Proteins).
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS (show FUS Proteins) act in a pathogenic pathway that is independent of SOD1 (show SOD1 Proteins).
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20.
TAR DNA binding protein
, TAR DNA-binding protein 43
, Tardbp protein
, TAR DNA-binding protein-43