scholarly journals The role of transcriptional factor D-site-binding protein in circadian CCL2 gene expression in anti-Thy1 nephritis

2018 ◽  
Vol 16 (9) ◽  
pp. 735-745 ◽  
Author(s):  
Yang Lu ◽  
Yan Mei ◽  
Lei Chen ◽  
Lingling Wu ◽  
Xu Wang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Transcriptional Factor ◽  
Ccl2 Gene ◽  
Site Binding

scholarly journals KH-type splicing regulatory protein is a new component of chromatoid body

Reproduction ◽  
2017 ◽  
Vol 154 (6) ◽  
pp. 723-733 ◽  
Author(s):  
Huijuan Zhang ◽  
Guishuan Wang ◽  
Lin Liu ◽  
Xiaolin Liang ◽  
Yu Lin ◽  
...  
Keyword(s):  
Gene Expression ◽  
Germ Cell ◽  
Knockout Mice ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Somatic Cells ◽  
Chromatoid Body ◽  
Mechanistic Insight ◽  
Insight Into

The chromatoid body (CB) is a specific cloud-like structure in the cytoplasm of haploid spermatids. Recent findings indicate that CB is identified as a male germ cell-specific RNA storage and processing center, but its function has remained elusive for decades. In somatic cells, KH-type splicing regulatory protein (KSRP) is involved in regulating gene expression and maturation of select microRNAs (miRNAs). However, the function of KSRP in spermatogenesis remains unclear. In this study, we showed that KSRP partly localizes in CB, as a component of CB. KSRP interacts with proteins (mouse VASA homolog (MVH), polyadenylate-binding protein 1 (PABP1) and polyadenylate-binding protein 2 (PABP2)), mRNAs (Tnp2 and Odf1) and microRNAs (microRNA-182) in mouse CB. Moreover, KSRP may regulate the integrity of CB via DDX5-miRNA-182 pathway. In addition, we found abnormal expressions of CB component in testes of Ksrp-knockout mice and of patients with hypospermatogenesis. Thus, our results provide mechanistic insight into the role of KSRP in spermatogenesis.

Poly(A)-binding protein (PABP): a common viral target

2010 ◽  
Vol 426 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Richard W. P. Smith ◽  
Nicola K. Gray
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Intracellular Localization ◽  
Mrna Translation ◽  
Dna Viruses ◽  
Multifunctional Protein ◽  
Wide Range ◽  
Viral Target ◽  
Rna And Dna

Cytoplasmic PABP [poly(A)-binding protein] is a multifunctional protein with well-studied roles in mRNA translation and stability. In the present review, we examine recent evidence that the activity of PABP is altered during infection with a wide range of viruses, bringing about changes in its stability, complex formation and intracellular localization. Targeting of PABP by both RNA and DNA viruses highlights the role of PABP as a central regulator of gene expression.

scholarly journals 5-hydroxymethylcytosine accumulation in postmitotic neurons results in functional demethylation of expressed genes

2017 ◽  
Vol 114 (37) ◽  
pp. E7812-E7821 ◽  
Author(s):  
Marian Mellén ◽  
Pinar Ayata ◽  
Nathaniel Heintz
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Binding Specificity ◽  
Chromatin Organization ◽  
Postmitotic Neurons ◽  
Cg Dinucleotides

5-hydroxymethylcytosine (5hmC) occurs at maximal levels in postmitotic neurons, where its accumulation is cell-specific and correlated with gene expression. Here we demonstrate that the distribution of 5hmC in CG and non-CG dinucleotides is distinct and that it reflects the binding specificity and genome occupancy of methylcytosine binding protein 2 (MeCP2). In expressed gene bodies, accumulation of 5hmCG acts in opposition to 5mCG, resulting in “functional” demethylation and diminished MeCP2 binding, thus facilitating transcription. Non-CG hydroxymethylation occurs predominantly in CA dinucleotides (5hmCA) and it accumulates in regions flanking active enhancers. In these domains, oxidation of 5mCA to 5hmCA does not alter MeCP2 binding or expression of adjacent genes. We conclude that the role of 5-hydroxymethylcytosine in postmitotic neurons is to functionally demethylate expressed gene bodies while retaining the role of MeCP2 in chromatin organization.

scholarly journals Induction of utrophin gene expression by heregulin in skeletal muscle cells: Role of the N-box motif and GA binding protein

1999 ◽  
Vol 96 (6) ◽  
pp. 3223-3227 ◽  
Author(s):  
A. O. Gramolini ◽  
L. M. Angus ◽  
L. Schaeffer ◽  
E. A. Burton ◽  
J. M. Tinsley ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Binding Protein ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Ga Binding Protein

scholarly journals Flexible phase adjustment of circadian albumin D site-binding protein (Dbp) gene expression by CRYPTOCHROME1

2010 ◽  
Vol 24 (12) ◽  
pp. 1317-1328 ◽  
Author(s):  
M. Stratmann ◽  
F. Stadler ◽  
F. Tamanini ◽  
G. T. J. van der Horst ◽  
J. A. Ripperger
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Phase Adjustment ◽  
Site Binding

scholarly journals Targeted Knockdown of RNA-Binding Protein TIAR for Promoting Self-Renewal and Attenuating Differentiation of Mouse Embryonic Stem Cells

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Zhe Geng ◽  
Ping Li ◽  
Li Tan ◽  
Houyan Song
Keyword(s):  
Gene Expression ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Embryonic Stem ◽  
Genetic Rescue ◽  
Self Renewal ◽  
Translational Level ◽  
Gene Expression Levels

RNA-binding protein TIAR has been suggested to mediate the translational silencing of ARE-containing mRNAs. To analyze the functions of TIAR, we established RNAi and genetic rescue assays. We evaluated the expression of neuroectoderm markers Pax6 and nestin, mesoderm markers brachyury and Flk1, and hypoblast and definitive endoderm markers Sox17 and Gata6 during EB differentiation and found that knockdown TIAR expression restrained the differentiation of E14 cells. We assessed gene expression levels of Flk-1 and VE-cadherin and observed attenuated differentiation of E14 cells into endothelial cells upon downregulation of TIAR gene expression. As such, we hypothesized an essential role of TIAR related to EB differentiation. As TIAR inhibits the translation of c-myc, we proposed that downregulation of TIAR results in restrained differentiation of E14 cells, due in part to the function of c-myc. We found that TIAR inhibited c-myc expression at the translational level in E14 cells; accordingly, a reduction of TIAR expression promoted self-renewal of pluripotent cells and attenuated differentiation. Additionally, we established that TIAR inhibited TIA-1 expression at the translational level in E14 cells. Taken together, we have contributed to the understanding of the regulatory relationships between TIAR and both c-myc and TIA-1.

Regulation of sterol regulatory-element binding protein 1 gene expression in liver: role of insulin and protein kinase B/cAkt

2000 ◽  
Vol 349 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Mark FLEISCHMANN ◽  
Patrick B. IYNEDJIAN
Keyword(s):  
Gene Expression ◽  
Protein Kinase ◽  
Recombinant Protein ◽  
Protein Kinase B ◽  
Binding Protein ◽  
Regulatory Element ◽  
Mutant Form ◽  
Element Binding Protein ◽  
Sterol Regulatory Element

Insulin stimulates the transcription of the sterol regulatory- element binding protein (SREBP) 1/ADD1 gene in liver. Hepatocytes in primary culture were used to delineate the insulin signalling pathway for induction of SREBP1 gene expression. The inhibitors of phosphoinositide 3-kinase (PI 3-kinase), wortmannin and LY 294002, abolished the insulin-dependent increase in SREBP1 mRNA, whereas the inhibitor of the mitogen- activated protein kinase cascade, PD 98059, was without effect. To investigate the role of protein kinase B (PKB)/cAkt downstream of PI 3-kinase, hepatocytes were transduced with an adenovirus encoding a PKB-oestrogen receptor fusion protein. The PKB activity of this recombinant protein was rapidly activated in hepatocytes challenged with 4-hydroxytamoxifen (OHT), as was endogenous PKB in hepatocytes challenged with insulin. The addition of OHT to transduced hepatocytes resulted in accumulation of SREBP1 mRNA, with a time-course and magnitude similar to the effect of insulin in non-transduced cells. The level of SREBP1 mRNA was not increased by OHT in hepatocytes expressing a mutant form of the recombinant protein whose PKB activity was not activated by OHT. Thus acute activation of PKB is sufficient to induce SREBP1 mRNA accumulation in primary hepatocytes, and might be the major signalling event by which insulin induces SREBP1 gene expression in the liver.

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