A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP
about
Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicingRBT1, a novel transcriptional co-activator, binds the second subunit of replication protein ALINE-1 ORF1 protein localizes in stress granules with other RNA-binding proteins, including components of RNA interference RNA-induced silencing complexEWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes.Identification of novel stress-induced genes downstream of chopTLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis.TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteinsALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear importTLS inhibits RNA polymerase III transcriptionRoles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulationMechanisms of FUS mutations in familial amyotrophic lateral sclerosisHuman 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formationIdentification of an RNA binding specificity for the potential splicing factor TLSThe N-terminal domain of human TAFII68 displays transactivation and oncogenic propertiesThe splicing factor U1C represses EWS/FLI-mediated transactivationCHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activationInvolvement of the pro-oncoprotein TLS (translocated in liposarcoma) in nuclear factor-kappa B p65-mediated transcription as a coactivatorThe prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domainGene amplification and associated loss of 5' regulatory sequences of CoAA in human cancersThe transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLSDomain architectures and characterization of an RNA-binding protein, TLSCHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulumStress-induced binding of the transcriptional factor CHOP to a novel DNA control elementCHOP-Dependent stress-inducible expression of a novel form of carbonic anhydrase VIEWS and FUS bind a subset of transcribed genes encoding proteins enriched in RNA regulatory functionsStructural and functional analysis of interferon regulatory factor 3: localization of the transactivation and autoinhibitory domainsFUS is sequestered in nuclear aggregates in ALS patient fibroblasts.Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity.FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stressPhosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains.Gene expression responses to FUS, EWS, and TAF15 reduction and stress granule sequestration analyses identifies FET-protein non-redundant functions.FUS-DDIT3 prevents the development of adipocytic precursors in liposarcoma by repressing PPARgamma and C/EBPalpha and activating eIF4E.The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response.Translocations, cancer and the puzzle of specificity.The C/EBP family of transcription factors in the liver and other organs.Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer.Fusion of the RBP56 and CHN genes in extraskeletal myxoid chondrosarcomas with translocation t(9;17)(q22;q11).Cell senescence in myxoid/round cell liposarcomaInhibition of CHOP translation by a peptide encoded by an open reading frame localized in the chop 5'UTRDual transforming activities of the FUS (TLS)-ERG leukemia fusion protein conferred by two N-terminal domains of FUS (TLS).
P2860
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P2860
A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP
description
1994 nî lūn-bûn
@nan
1994 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
A novel effector domain from t ...... cogenic transformation by CHOP
@ast
A novel effector domain from t ...... cogenic transformation by CHOP
@en
A novel effector domain from t ...... cogenic transformation by CHOP
@nl
type
label
A novel effector domain from t ...... cogenic transformation by CHOP
@ast
A novel effector domain from t ...... cogenic transformation by CHOP
@en
A novel effector domain from t ...... cogenic transformation by CHOP
@nl
prefLabel
A novel effector domain from t ...... cogenic transformation by CHOP
@ast
A novel effector domain from t ...... cogenic transformation by CHOP
@en
A novel effector domain from t ...... cogenic transformation by CHOP
@nl
P2860
P356
P1433
P1476
A novel effector domain from t ...... cogenic transformation by CHOP
@en
P2093
P2860
P304
P356
10.1101/GAD.8.21.2513
P407
P50
P577
1994-11-01T00:00:00Z