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PTBP1 (show PTBP1 Proteins) and PTBP2 impaired autoregulation of SRSF3 (show SRSF3 Proteins) in oral squamous cell carcinoma cancer cells.
Data show that polypyrimidine tract-binding (show PTBP1 Proteins) proteins nPTB and ROD1 (show PTBP3 Proteins) interact with mitochondrial tRNA(Thr (show TRH Proteins)) in the cytoplasm outside of mitochondria.
In T98G glioma cells, the level of sumoylated PTBP2 was reduced compared to that of normal brain cells. Overall, this study shows that PTBP2 is posttranslationally modified by SUMO1 (show SUMO1 Proteins).
MALAT1 binds to SFPQ releasing PTBP2 from the SFPQ/PTBP2 complex, the increased SFPQ-detached PTBP2 promotes cell proliferation and migration in colorectal cancer.
Defining the multifunctional roles of PTB (show PTBP1 Proteins) will contribute to the understanding of key regulatory events in gene expression.
Changes in miR (show MLXIP Proteins)-223/PTBP2 pathway could contribute of abnormal splicing in chronic myeloid leukemia (show BCL11A Proteins).
Regulation of the mutually exclusive exons 8a and 8 in the CaV1.2 (show CACNA1C Proteins) calcium channel transcript by polypyrimidine tract-binding protein (show PTBP1 Proteins).
present fluorescence, NMR, and in vivo splicing data in support of a role of PTB (show PTBP1 Proteins) in inducing RNA loops. We show that the RNA recognition motifs (RRMs) 3 and 4 of PTB (show PTBP1 Proteins) can bind two distant pyrimidine tracts and bring their 5' and 3' ends in close proximity
The nPTB proximal promoter, although rich in G+C content and presenting putative binding sites for the transcription factors Sp1 (show PSG1 Proteins), NF-1 (show NF1 Proteins), NF-kB and Oct-1 (show POU2F1 Proteins), lacks a typical TATA box.
Study shows that PTB (show PTBP1 Proteins) can function as an anti-repressor molecule to counteract the splicing inhibitory activity of SRp30c (show SFRS9 Proteins).
Ptbp2 ablation results in germ cell loss due to increased apoptosis of meiotic spermatocytes and postmeiotic arrest of spermatid differentiation.
These results define a new genetic regulatory program, where PTBP2 acts to temporarily repress expression of adult protein isoforms until the final maturation of the neuron.
Thus, Ptbp2 inhibition of a discrete set of adult neuronal exons underlies early brain development prior to neuronal differentiation and is essential for postnatal survival.
The expression of PSD-95 (show DLG4 Proteins) during early neural development is controlled at the RNA level by two PTB (show PTBP1 Proteins) proteins whose sequential downregulation is necessary for synapse maturation.
The present study provides evidence that alternative neuronal nPTB and Fox-1 (show A2BP1 Proteins)/Fox-2 (show RBM9 Proteins) isoforms are also produced in lenses
Reduction of PTBP2 levels led to decreases in 7 of 10 of the mRNAs, to the repression of alternative splicing of introns, and to reductions in specific miRNAs.
The predominant expression of REST4, HuB/C/D and nPTB in post-mitotic fiber cells, together with miR (show MLXIP Proteins)-124 expression in vertebrate lenses, was shown.
PTBP2 is a trans-acting factor that helps to stabilize Pgk2 (show PGK2 Proteins) mRNA in male mouse germ cells.
The post-transcriptional switch from PTB (show PTBP1 Proteins) to nPTB controls a widespread alternative splicing program during neuronal development.
Two stretches of polypyrimidine tracts designated PPT1 and PPT2 which influence the IRES activity of cx55.5 protein were identified; deletion of PPT2 results in a complete loss of the IRES activity
The protein encoded by this gene binds to the intronic cluster of RNA regulatory elements, downstream control sequence (DCS). It is implicated in controlling the assembly of other splicing-regulatory proteins. This protein is very similar to the polypyrimidine tract binding protein but it is expressed primarily in the brain.
polypyrimidine tract binding protein 2
, polypyrimidine tract-binding protein 2-like
, PTB-like protein
, neural polypyrimidine tract binding protein
, neural polypyrimidine tract-binding protein
, neurally-enriched homolog of PTB
, polypyrimidine tract-binding protein 2
, splicing regulator
, RRM-type RNA-binding protein brPTB
, brain-enriched PTB
, brain-enriched polypyrimidine tract-binding protein