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FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Zusätzlich bieten wir Ihnen FUS Antikörper (39) und FUS Kits (3) und viele weitere Produktgruppen zu diesem Protein an.
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Human FUS Protein expressed in HEK-293 Cells - ABIN2721461
Groen, Fumoto, Blokhuis, Engelen-Lee, Zhou, van den Heuvel, Koppers, van Diggelen, van Heest, Demmers, Kirby, Shaw, Aronica, Spliet, Veldink, van den Berg, Pasterkamp: ALS-associated mutations in FUS disrupt the axonal distribution and function of SMN. in Human molecular genetics 2013
Show all 3 Pubmed References
more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS than in FTLD-tau
Taken together, FUS RNA-recognition motif appears to play a crucial role in exaggerating the physiological/reversible self-assembly into pathological/irreversible fibrillization, thus contributing to manifestation of FUS cytotoxicity.
Fus is a binding partner of FMRP (zeige FMR1 Proteine).
Study demonstrates that FUS mutants, but not WT forms, impair fast axonal transport (FAT) in brain tissue of patients with ALS (zeige IGFALS Proteine), through a mechanism dependent on activation of p38 MAPK (zeige MAPK14 Proteine).
In human stem (zeige TAF15 Proteine) cell-derived motor neurons, the RNA profile associated with concomitant loss of both TAF15 and FUS resembles that observed in the (zeige TAF15 Proteine)presence of the amyotrophic lateral sclerosis (ALS)-associated mutation FUS R521G, but co (zeige TARDBP Proteine)ntrasts with late-stage sporadic ALS patients.
FUS P525L mutation alters transcriptome and microRNA pathways in motor neurons with implications for ALS pathogenesis.
This study showed that in fibroblasts of FUS P525L mutation carriers, FUS mislocalized to the cytoplasm where it redistributed into stress granules with likely a dose effect.
Results find that mutant but not wild-type FUS decreased dendritic growth, mRNA levels, and protein synthesis in dendrites. These data suggest that cytoplasmic FUS aggregates trap mRNA and its transporters, impairing dendritic mRNA trafficking and translation, in turn leading to the disruption of dendritic homeostasis and the development of frontotemporal dementia phenotypes.
activation of the IGF-IR/PI3K (zeige PIK3CA Proteine)/Akt (zeige AKT1 Proteine) signaling system is a common pattern in MLS which appears to be transcriptionally controlled, at least in part by induction of IGF2 gene transcription in a FUS-DDIT3 (zeige DDIT3 Proteine)-dependent manner.
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 and TAF15 (zeige TAF15 Proteine) exhibit similar global RNA interaction profiles in vivo, but affect a strikingly small subset of common genes. Unexpectedly, TAF15 (zeige TAF15 Proteine) influences a small fraction of amyotrophic lateral sclerosis events compared with TDP-43 (zeige TARDBP Proteine) and FUS in the mouse CNS.
FUS and the ELAV (zeige ELAVL4 Proteine)-like proteins ELAVL4 (zeige ELAVL4 Proteine) and ELAVL1 (zeige ELAVL1 Proteine) control SynGAP (zeige SYNGAP1 Proteine) mRNA stability in a 3'UTR length-dependent manner, resulting in the stable expression of the alternatively spliced SynGAP (zeige SYNGAP1 Proteine) isoform alpha2.
These two proteins were up-regulated in both HD and FUS/TLS heterozygote mice.
Study established that Fus1 (zeige TUSC2 Proteine) KO mice suffer from the age-related hearing loss (ARHL) of strial origin, making this model a valuable tool for studying mitochondrial/oxidative mechanisms of age-related hearing decline. The model describes the phenotype of premature hearing loss of strial etiology based on Fus1 (zeige TUSC2 Proteine) loss-mediated mitochondrial dysfunction, and identify the target cells and tissues in the inner ear.
Authors found that FUS, EWS (zeige EWSR1 Proteine) and TAF15 (zeige TAF15 Proteine) expression is differentially regulated during brain development, both in time and in space. In particular, this study identifies a fine-tuned regulation of FUS and EWS (zeige EWSR1 Proteine) during neuronal differentiation.
Study characterizes a heterozygous knock-in mouse model of ALS and demonstrates that mutations in FUS result in a toxic gain of function leading to motor neuron disease through cell autonomous and non-cell autonomous mechanisms; shows that mutant FUS triggers toxic events in both motor neurons and neighboring cells to elicit motor neuron disease.
FUS-induced reductions to ER-mitochondria associations and are linked to activation of glycogen synthase kinase-3beta (GSK-3beta), a kinase already strongly associated with ALS/FTD (zeige FTL Proteine).
our findings indicate that cytoplasmic FUS mislocalization not only leads to nuclear loss of function, but also triggers motor neuron death through a toxic gain of function within motor neurons.
The data of this study support the notion that expression of cytoplasmically mislocalized FUS with compromised RNA-binding capacity causes particularly prominent and harmful FUS pathology in the mouse nervous system.
These results highlight the pivotal role of FUS in regulating GluA1 (zeige GRIA1 Proteine) mRNA stability, post-synaptic function and fronto-temporal lobar degeneration-like animal behaviors.
This gene encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The hnRNP complex is involved in pre-mRNA splicing and the export of fully processed mRNA to the cytoplasm. This protein belongs to the FET family of RNA-binding proteins which have been implicated in cellular processes that include regulation of gene expression, maintenance of genomic integrity and mRNA/microRNA processing. Alternative splicing results in multiple transcript variants. Defects in this gene result in amyotrophic lateral sclerosis type 6.
75 kDa DNA-pairing protein
, RNA-binding protein FUS
, fus-like protein
, fusion gene in myxoid liposarcoma
, heterogeneous nuclear ribonucleoprotein P2
, oncogene FUS
, oncogene TLS
, translocated in liposarcoma protein
, fusion, derived from t(12;16) malignant liposarcoma
, hnRNP P2
, pigpen protein
, protein pigpen
, translocated in liposarcoma
, fusion (involved in t(12;16) in malignant liposarcoma)
, 16) in malignant liposarcoma)
, 16) malignant liposarcoma
, fusion (involved in t(12
, fusion, derived from t(12