scholarly journals Triphenyltin inhibits GA-binding protein α nuclear translocation

2020 ◽  
Vol 7 (1) ◽  
pp. 33-40
Author(s):  
Naohiro Kidoguchi ◽  
Keishi Ishida ◽  
Seigo Sanoh ◽  
Masatsugu Miyara ◽  
Yaichiro Kotake
Keyword(s):  
Nuclear Translocation ◽  
Binding Protein ◽  
Ga Binding Protein

scholarly journals Transcriptional regulation of importin-α1 by JunD modulates subcellular localization of RNA-binding protein HuR in intestinal epithelial cells

2016 ◽  
Vol 311 (6) ◽  
pp. C874-C883 ◽  
Author(s):  
Yan Xu ◽  
Jie Chen ◽  
Lan Xiao ◽  
Hee Kyoung Chung ◽  
Yuan Zhang ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Subcellular Localization ◽  
Rna Binding ◽  
Nuclear Translocation ◽  
Intestinal Epithelial Cells ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Intestinal Epithelial ◽  
Mucosal Regeneration ◽  
Importin Α

The RNA-binding protein HuR is crucial for normal intestinal mucosal regeneration by modulating the stability and translation of target mRNAs, but the exact mechanism underlying HuR trafficking between the cytoplasm and nucleus remains largely unknown. Here we report a novel function of transcription factor JunD in the regulation of HuR subcellular localization through the control of importin-α1 expression in intestinal epithelial cells (IECs). Ectopically expressed JunD specifically inhibited importin-α1 at the transcription level, and this repression is mediated via interaction with CREB-binding site that was located at the proximal region of importin-α1 promoter. Reduction in the levels of importin-α1 by JunD increased cytoplasmic levels of HuR, although it failed to alter whole cell HuR levels. Increased levels of endogenous JunD by depleting cellular polyamines also inhibited importin-α1 expression and increased cytoplasmic HuR levels, whereas JunD silencing rescued importin-α1 expression and enhanced HuR nuclear translocation in polyamine-deficient cells. Moreover, importin-α1 silencing protected IECs against apoptosis, which was prevented by HuR silencing. These results indicate that JunD regulates HuR subcellular distribution by downregulating importin-α1, thus contributing to the maintenance of gut epithelium homeostasis.

scholarly journals GA-Binding Protein Is Dispensable for Neuromuscular Synapse Formation and Synapse-Specific Gene Expression

2007 ◽  
Vol 27 (13) ◽  
pp. 5040-5046 ◽  
Author(s):  
Alexander Jaworski ◽  
Cynthia L. Smith ◽  
Steven J. Burden
Keyword(s):  
Gene Expression ◽  
Synapse Formation ◽  
Binding Protein ◽  
Neuromuscular Synapse ◽  
Specific Gene ◽  
Promoter Regions ◽  
Specific Gene Expression ◽  
Muscle Gene Expression ◽  
Synaptic Region ◽  
Ga Binding Protein

ABSTRACT The mRNAs encoding postsynaptic components at the neuromuscular junction are concentrated in the synaptic region of muscle fibers. Accumulation of these RNAs in the synaptic region is mediated, at least in part, by selective transcription of the corresponding genes in synaptic myofiber nuclei. The transcriptional mechanisms that are responsible for synapse-specific gene expression are largely unknown, but an Ets site in the promoter regions of acetylcholine receptor (AChR) subunit genes and other “synaptic” genes is required for synapse-specific transcription. The Ets domain transcription factor GA-binding protein (GABP) has been implicated to mediate synapse-specific gene expression. Inactivation of GABPα, the DNA-binding subunit of GABP, leads to early embryonic lethality, preventing analysis of synapse formation in gabpα mutant mice. To study the role of GABP at neuromuscular synapses, we conditionally inactivated gabpα in skeletal muscle and studied synaptic differentiation and muscle gene expression. Although expression of rb, a target of GABP, is elevated in muscle tissue deficient in GABPα, clustering of synaptic AChRs at synapses and synapse-specific gene expression are normal in these mice. These data indicate that GABP is dispensable for synapse-specific transcription and maintenance of normal AChR expression at synapses.

scholarly journals Cytoplasmic Sequestration of the Polyomavirus Enhancer Binding Protein 2 (PEBP2)/Core Binding Factor α (CBFα) Subunit by the Leukemia-Related PEBP2/CBFβ-SMMHC Fusion Protein Inhibits PEBP2/CBF-Mediated Transactivation

1998 ◽  
Vol 18 (7) ◽  
pp. 4252-4261 ◽  
Author(s):  
Yuka Kanno ◽  
Tomohiko Kanno ◽  
Chohei Sakakura ◽  
Suk-Chul Bae ◽  
Yoshiaki Ito
Keyword(s):  
Nuclear Translocation ◽  
Binding Protein ◽  
Myelogenous Leukemia ◽  
Luciferase Assay ◽  
Β Subunit ◽  
Core Binding Factor ◽  
Α Subunit ◽  
Enhancer Binding Protein ◽  
Binding Factor ◽  
Minimal Region

ABSTRACT The polyomavirus enhancer binding protein 2 (PEBP2)/core binding factor (CBF) is a transcription factor composed of two subunits, α and β. The gene encoding the β subunit is disrupted by inv(16), resulting in the formation of a chimeric protein, β-SMMHC, which is associated with acute myelogenous leukemia. To understand the effect of β-SMMHC on PEBP2-mediated transactivation, we used a luciferase assay system in which contribution of both the α and β subunits was absolutely required to activate transcription. Using this system, we found that the minimal region of the β subunit required for transactivation resides between amino acid 1 and 135, which is known to dimerize with the α subunit. In contrast, β-SMMHC, despite having this minimal region for dimerization and transactivation, failed to support transcription with the α subunit. Furthermore β-SMMHC blocked the synergistic transcription achieved by PEBP2 and CCAAT/enhancer binding protein α. By using a construct in which the PEBP2 α subunit was fused to the glucocorticoid receptor ligand binding domain, we demonstrated that coexpressed β-SMMHC tightly sequestered the α subunit in the cytoplasm and blocked dexamethasone-dependent nuclear translocation of the α subunit. Thus, the result suggess that β-SMMHC inhibits PEBP2-mediated transcription via cytoplasmic sequestration of the α subunit. Lastly proliferation of ME-1 cells that harbor inv(16) was blocked by an antisense oligonucleotide complementary to the junction of the chimeric mRNA, suggesting that β-SMMHC contributes to leukemogenesis by blocking the differentiation of myeloid cells.

scholarly journals Redox Regulation of GA-binding Protein-α DNA Binding Activity

1996 ◽  
Vol 271 (41) ◽  
pp. 25617-25623 ◽  
Author(s):  
Mark E. Martin ◽  
Yurii Chinenov ◽  
Mi Yu ◽  
Tonya K. Schmidt ◽  
Xiu-Ying Yang
Keyword(s):  
Dna Binding ◽  
Redox Regulation ◽  
Binding Protein ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Ga Binding Protein

scholarly journals GA binding protein augments autophagy via transcriptional activation ofBECN1-PIK3C3complex genes

Autophagy ◽  
2014 ◽  
Vol 10 (9) ◽  
pp. 1622-1636 ◽  
Author(s):  
Wan Zhu ◽  
Gayathri Swaminathan ◽  
Edward D Plowey
Keyword(s):  
Transcriptional Activation ◽  
Binding Protein ◽  
Ga Binding Protein

scholarly journals Is PPARβ/δa Retinoid Receptor?

PPAR Research ◽  
2007 ◽  
Vol 2007 ◽  
pp. 1-5 ◽  
Author(s):  
Daniel C. Berry ◽  
Noa Noy
Keyword(s):  
Retinoic Acid ◽  
Fatty Acid Binding Protein ◽  
Nuclear Translocation ◽  
Retinoic Acid Receptor ◽  
Binding Protein ◽  
Retinoid Receptor ◽  
Expression Ratio ◽  
Fatty Acid Binding ◽  
Bona Fide ◽  
Crabp Ii

The broad ligand-binding characteristic of PPARβ/δhas long hampered identification of physiologically-meaningful ligands for the receptor. The observations that the activity of PPARβ/δis supported by fatty acid binding protein 5 (FABP5), which directly delivers ligands from the cytosol to the receptor, suggest thatbona fidePPARβ/δligands both activate the receptor, and trigger the nuclear translocation of FABP5. Using these criteria, it was recently demonstrated that all-trans-retinoic acid (RA), the activator of the classical retinoic acid receptor RAR, also serves as a ligand for PPARβ/δ. Partitioning of RA between its two receptors was found to be regulated by FABP5, which delivers it to PPARβ/δ, and cellular RA binding protein II (CRABP-II), which targets it to RAR. Consequently, RA activates PPARβ/δin cells that display a high FABP5/CRABP-II expression ratio. It remains to be clarified whether compounds other than RA may also serve as endogenous activators for this highly promiscuous protein.

scholarly journals Author Correction: Up regulation and nuclear translocation of Y-box binding protein 1 (YB-1) is linked to poor prognosis in ERG-negative prostate cancer

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Asmus Heumann ◽  
Özge Kaya ◽  
Christoph Burdelski ◽  
Claudia Hube-Magg ◽  
Martina Kluth ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Poor Prognosis ◽  
Nuclear Translocation ◽  
Binding Protein

scholarly journals GA-binding protein GABPβ1 is required for the proliferation of neural stem/progenitor cells

2019 ◽  
Vol 39 ◽  
pp. 101501 ◽  
Author(s):  
Cong Liu ◽  
Shang-Kun Dai ◽  
Zhen Sun ◽  
Zhuo Wang ◽  
Pei-Pei Liu ◽  
...  
Keyword(s):  
Progenitor Cells ◽  
Binding Protein ◽  
Neural Stem Progenitor Cells ◽  
Ga Binding Protein
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