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Polypyrimidine tract binding protein 1

PTB, Heterogeneous-Nuclear Ribonucleoprotein, Polypyrimidine Tract-Binding Protein
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, V1a, ACID, Src
Papers using PTB antibodies
Cleavage Map and Proteolytic Processing of the Murine Norovirus Nonstructural Polyprotein in Infected Cells.
Supplier
Ryu Wang-Shick, In PLoS ONE, 2005
... Antisera for western blot to hnRNP I (PTB) was purchased from Santa Cruz Biotechnology, mouse monoclonal antibodies to ...
Autoregulation of polypyrimidine tract binding protein by alternative splicing leading to nonsense-mediated decay
Supplier
Tarn Woan-Yuh et al., In The Journal of Cell Biology, 2003
... The His-tagged PTB expression vector was constructed by cloning the human PTB-coding region into pET-32a (QIAGEN).
Papers on PTB
Extra-pulmonary tuberculosis: a biomarker analysis.
New
Moreno et al., Madrid, Spain. In Infection, 21 Apr 2014
INTRODUCTION: Studies on biomarkers in tuberculosis are focused on pulmonary forms of this disease (PTB), and only limited information is currently available on biomarkers of extra-pulmonary tuberculosis (EPTB).
Association study of genes controlling IL-12-dependent IFN-γ immunity: STAT4 alleles increase risk of pulmonary tuberculosis in Morocco.
New
El Baghdadi et al., Rabat, Morocco. In J Infect Dis, 08 Apr 2014
Genetic epidemiological evidence suggests that pulmonary TB (PTB) has a strong human genetic component.
Phosphorylated c-MPL tyrosine 591 regulates thrombopoietin-induced signaling.
New
Hitchcock et al., Stony Brook, United States. In Exp Hematol, 04 Apr 2014
Using an SH2/PTB domain binding microarray, we identified novel c-MPL binding partners for phosphorylated Y591, including Src homology phosphatase-1 (SHP-1), spleen tyrosine kinase (SYK) and Bruton's tyrosine kinase (BTK).
Association of Mycobacterium Tuberculosis Lineages with IFN-γ and TNF-α Gene Polymorphisms among Pulmonary Tuberculosis Patient.
New
Velayati et al., Chābahār, Iran. In Mediterr J Hematol Infect Dis, Dec 2013
The results showed C allele of TNF 857 and A allele of TNF 238 were more frequent in PTB cases [[TNF 857 C allele OR [CI95%] 0.6[0.4-0.9],
Interferon-gamma treatment kinetics among patients with active pulmonary tuberculosis.
New
Obaseki et al., Nigeria. In Niger Med J, Nov 2013
The mean level of IFN-γ induced by TB antigens was 629 ± 114.1 pg/ml, higher for HIV-negative PTB patients compared with HIV-positive PTB patients, 609.78 ± 723.9 pg/ml and 87.88 ± 130.0 pg/ml, respectively, P-value = 0.000.
Acute effects of sildenafil and dobutamine in the hypertrophic and failing right heart in vivo.
New
Nielsen-Kudsk et al., Århus, Denmark. In Pulm Circ, Sep 2013
Wistar rats ([Formula: see text]) were subjected to pulmonary trunk banding (PTB) causing RV hypertrophy and failure.
PTB deficiency causes the loss of adherens junctions in the dorsal telencephalon and leads to lethal hydrocephalus.
New
GeneRIF
Yoshida et al., Tokyo, Japan. In Cereb Cortex, Aug 2013
PTB depletion in the dorsal telencephalon is causally involved in the development of hydrocephalus. And PTB is important for the maintenance of Adherens Junctions in the neural stem cells of the dorsal telencephalon.
Temporal regulation of EGF signalling networks by the scaffold protein Shc1.
New
Impact
Pawson et al., Toronto, Canada. In Nature, Aug 2013
Activated receptor tyrosine kinases, for example, engage scaffolds such as Shc1 that contain phosphotyrosine (pTyr)-binding (PTB) domains.
The insulin receptor: both a prototypical and atypical receptor tyrosine kinase.
Review
New
Hubbard, New York City, United States. In Cold Spring Harb Perspect Biol, Mar 2013
As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR's catalytic activity.
Direct conversion of fibroblasts to neurons by reprogramming PTB-regulated microRNA circuits.
New
Impact
Fu et al., Wuhan, China. In Cell, Feb 2013
Here, we report that repression of a single RNA binding polypyrimidine-tract-binding (PTB) protein, which occurs during normal brain development via the action of miR-124, is sufficient to induce trans-differentiation of fibroblasts into functional neurons.
Evolutionary dynamics of gene and isoform regulation in Mammalian tissues.
Impact
Burge et al., Cambridge, United States. In Science, 2013
Thousands of previously unknown, lineage-specific, and conserved alternative exons were identified; widely conserved alternative exons had signatures of binding by MBNL, PTB, RBFOX, STAR, and TIA family splicing factors, implicating them as ancestral mammalian splicing regulators.
ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect.
Impact
Lu et al., Houston, United States. In Nat Cell Biol, 2012
Nuclear PKM2 acts as a coactivator of β-catenin to induce c-Myc expression, resulting in the upregulation of GLUT1, LDHA and, in a positive feedback loop, PTB-dependent PKM2 expression.
Stem cell factor receptor/c-Kit: from basic science to clinical implications.
Review
Impact
Rönnstrand et al., Uppsala, Sweden. In Physiol Rev, 2012
Signaling proteins are recruited to activated c-Kit by certain interaction domains (e.g., SH2 and PTB) that specifically bind to phosphorylated tyrosine residues in the intracellular region of c-Kit.
Commentary: The carboxyl-terminal Crk SH3 domain: Regulatory strategies and new perspectives.
Review
Birge et al., Newark, United States. In Febs Lett, 2012
Moreover, SH3C is tyrosine phosphorylated by receptor tyrosine kinases and non-receptor tyrosine kinases, thereby permitting assemblages of other SH2/PTB domain containing proteins.
Defining the roles and interactions of PTB.
Review
Smith et al., Cambridge, United Kingdom. In Biochem Soc Trans, 2012
PTB (polypyrimidine tract-binding protein) is an abundant and widely expressed RNA-binding protein with four RRM (RNA recognition motif) domains.
From signal transduction to signal interpretation: an alternative model for the molecular function of insulin receptor substrates.
Review
Niessen et al., Zürich, Switzerland. In Arch Physiol Biochem, 2012
A family of IRS proteins was defined based on three major common structural elements: Amino-terminal PH and PTB domains that mediate protein-lipid or protein-protein interactions, mostly carboxy-terminal multiple tyrosine residues that serve as binding sites for proteins that contain one or more SH2 domains and serine/threonine-rich regions which may be recognized by negative regulators of insulin action.
The defective splicing caused by the ISCU intron mutation in patients with myopathy with lactic acidosis is repressed by PTBP1 but can be derepressed by IGF2BP1.
GeneRIF
Holmberg et al., Umeå, Sweden. In Hum Mutat, 2012
The defective splicing caused by the ISCU intron mutation in patients with myopathy with lactic acidosis is repressed by PTBP1 but can be derepressed by IGF2BP1.
PSD-95 is post-transcriptionally repressed during early neural development by PTBP1 and PTBP2.
GeneRIF
Black et al., Los Angeles, United States. In Nat Neurosci, 2012
The polypyrimidine tract binding proteins PTBP1 and PTBP2 repressed Psd-95 (also known as Dlg4) exon 18 splicing, leading to premature translation termination and nonsense-mediated mRNA decay.
Polypyrimidine tract binding protein (hnRNP I) is possibly a conserved modulator of miRNA-mediated gene regulation.
GeneRIF
Hutvagner et al., Dundee, United Kingdom. In Plos One, 2011
Polypyrimidine tract binding protein (hnRNP I) is possibly a conserved modulator of miRNA-mediated gene regulation.
Polypyrimidine tract-binding protein regulates the cell cycle through IRES-dependent translation of CDK11(p58) in mouse embryonic stem cells.
GeneRIF
Yoshida et al., Tokyo, Japan. In Cell Cycle, 2011
PTB regulates the precise expression of CDK11(p58) through direct interaction with CDK11(p58) IRES and promotes M phase progression in ES cells.
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