scholarly journals Poly C Binding Protein 2 dependent nuclear retention of the utrophin-A mRNA in C2C12 cells

RNA Biology ◽  
2021 ◽  
pp. 1-11
Author(s):  
Gargi Ghosh ◽  
Satyabrata Samui ◽  
Santanu Das ◽  
Vandana Singh ◽  
Doel Pal ◽  
...  
Keyword(s):  
Binding Protein ◽  
C2c12 Cells ◽  
Nuclear Retention

scholarly journals Inhibition of Transcription Induces Phosphorylation of YB-1 at Ser102 and Its Accumulation in the Nucleus

Cells ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 104 ◽  
Author(s):  
Dmitry A. Kretov ◽  
Daria A. Mordovkina ◽  
Irina A. Eliseeva ◽  
Dmitry N. Lyabin ◽  
Dmitry N. Polyakov ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rna Polymerase Ii ◽  
Nuclear Localization ◽  
Kinase Activity ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Regulatory Mechanisms ◽  
Nuclear Accumulation ◽  
Nuclear Retention ◽  
Post Translational Modifications

The Y-box binding protein 1 (YB-1) is an RNA/DNA-binding protein regulating gene expression in the cytoplasm and the nucleus. Although mostly cytoplasmic, YB-1 accumulates in the nucleus under stress conditions. Its nuclear localization is associated with aggressiveness and multidrug resistance of cancer cells, which makes the understanding of the regulatory mechanisms of YB-1 subcellular distribution essential. Here, we report that inhibition of RNA polymerase II (RNAPII) activity results in the nuclear accumulation of YB-1 accompanied by its phosphorylation at Ser102. The inhibition of kinase activity reduces YB-1 phosphorylation and its accumulation in the nucleus. The presence of RNA in the nucleus is shown to be required for the nuclear retention of YB-1. Thus, the subcellular localization of YB-1 depends on its post-translational modifications (PTMs) and intracellular RNA distribution.

Effect of mutation of amino acids 246–251 (KRKHKK) in HSP72 on protein synthesis and recovery from hypoxic injury

2005 ◽  
Vol 289 (6) ◽  
pp. H2519-H2525 ◽  
Author(s):  
M. R. Voss ◽  
S. Gupta ◽  
J. P. Stice ◽  
G. Baumgarten ◽  
L. Lu ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Dna Synthesis ◽  
Nuclear Localization ◽  
Nuclear Export ◽  
Cell Function ◽  
C2c12 Cells ◽  
Protective Effects ◽  
Nuclear Retention ◽  
Hypoxic Injury ◽  
Simulated Ischemia

Heat shock protein (HSP)72, the inducible form of HSP70, protects cells against a variety of injuries, but underlying mechanisms are poorly defined. To investigate the protective effects of HSP72, multiple clones expressing wild-type (WT) HSP72 and two mutants with defective nucleolar and nuclear localization (M45 and 985A, respectively) were made with the tet-off system in C2C12 cells. Four different parameters of cell function/injury were examined after simulated ischemia: protein synthesis, polysome formation, DNA synthesis, and lactate dehydrogenase (LDH release). Overexpression of WT HSP72 was also compared to nontransfected C2C12 cells. As expected, overexpression of HSP72 protected against simulated ischemia and reoxygenation for all parameters. In contrast, both M45 and 985A showed abnormal protein synthesis and polysome formation, both after simulated ischemia and under control conditions. Total RNA was slightly reduced in M45 and 985A at baseline, but 1 h after hypoxia, RNA levels were protected in all clones but significantly decreased in nontransfected C2C12 cells. Clones expressing 985A had nuclear retention of mRNA, suggesting that HSP72 is needed for nuclear export of RNA. All clones, both WT and mutant, had protection of DNA synthesis compared to C2C12 cells, but 985A had greater release of LDH after injury than any other group. These results support a multifactoral protective effect of HSP72, some aspects dependent on nuclear localization with stress and some not. The protection of protein synthesis and polysome formation, and abnormalities in these with the mutants, support a role for HSP72 in these processes both in the normal cell and in injury.

scholarly journals The role of Ran-binding protein 3 during influenza A virus replication

2013 ◽  
Vol 94 (5) ◽  
pp. 977-984 ◽  
Author(s):  
Rey Predicala ◽  
Yan Zhou
Keyword(s):  
Life Cycle ◽  
Influenza A Virus ◽  
Nuclear Export ◽  
Influenza A ◽  
Binding Protein ◽  
Late Phase ◽  
Nuclear Retention ◽  
Interacting Protein ◽  
Virus Life Cycle

Influenza A virus vRNP nuclear export is CRM1-dependent. Ran-binding protein 3 (RanBP3) is a Ran-interacting protein that is best known for its role as a cofactor of CRM1-mediated cargo nuclear export. In this study, we investigated the role of RanBP3 during the influenza A virus life cycle. We found that RanBP3 was phosphorylated at Ser58 in the early and late phases of infection. Knockdown of RanBP3 expression led to vRNP nuclear retention, suggesting that RanBP3 is involved in vRNP nuclear export. Moreover, we demonstrated that the function of RanBP3 during vRNP nuclear export is regulated by phosphorylation at Ser58, and that RanBP3 phosphorylation is modulated by both PI3K/Akt and Ras/ERK/RSK pathways in the late phase of viral infection.

scholarly journals Nuclear Import of Cytoplasmic Poly(A) Binding Protein Restricts Gene Expression via Hyperadenylation and Nuclear Retention of mRNA

2010 ◽  
Vol 30 (21) ◽  
pp. 4996-5008 ◽  
Author(s):  
G. Renuka Kumar ◽  
Britt A. Glaunsinger
Keyword(s):  
Gene Expression ◽  
Binding Protein ◽  
Tail Length ◽  
Nuclear Accumulation ◽  
Cellular Gene ◽  
Nuclear Retention ◽  
Signal Degradation ◽  
Mrna Fate ◽  
Influence Gene Expression ◽  
Important Marker

ABSTRACT Poly(A) tail length is emerging as an important marker of mRNA fate, where deviations from the canonical length can signal degradation or nuclear retention of transcripts. Pathways regulating polyadenylation thus have the potential to broadly influence gene expression. Here we demonstrate that accumulation of cytoplasmic poly(A) binding protein (PABPC) in the nucleus, which can occur during viral infection or other forms of cellular stress, causes mRNA hyperadenylation and nuclear accumulation of poly(A) RNA. This inhibits gene expression but does not affect mRNA stability. Unexpectedly, PABPC-induced hyperadenylation can occur independently of mRNA 3′-end processing yet requires the canonical mRNA poly(A) polymerase II. We find that nuclear PABPC-induced hyperadenylation is triggered by multiple divergent viral factors, suggesting that altering the subcellular localization of PABPC may be a commonly used mechanism to regulate cellular gene expression in a polyadenylation-linked manner.

Msx3 protein recruits histone deacetylase to down-regulate the Msx1 promoter

2000 ◽  
Vol 353 (1) ◽  
pp. 13-22 ◽  
Author(s):  
Ritcha MEHRA-CHAUDHARY ◽  
Hideo MATSUI ◽  
Rajendra RAGHOW
Keyword(s):  
Histone Deacetylase ◽  
Binding Protein ◽  
Trichostatin A ◽  
Camp Response Element Binding ◽  
C2c12 Cells ◽  
Dependent Manner ◽  
Camp Response Element ◽  
Histone Deacetylase 1 ◽  
Element Binding Protein ◽  
Dual Mechanism

Msx1 promoter is known to be repressed by Msx1 protein [Shetty, Takahashi, Matsui, Iyengar and Raghow (1999) Biochem. J. 339, 751–758]. We show that in the transiently transfected C2C12 myoblasts, co-expression of Msx3 also causes potent repression of Msx1 promoter that can be relieved by exogenous expression of cAMP-response-element-binding protein-binding protein (CBP) and p300 in a dose-dependent manner. Co-immunoprecipitation and Western blot analyses revealed that Msx3 interacts with CBP and p300 and this interaction significantly decreases the histone acetyltransferase (HAT) activity of both proteins. We also discovered that Msx3-mediated repression of Msx1 promoter is synergized by the exogenous co-expression of histone deacetylase 1 (HDAC1). Furthermore, the repression of Msx1 promoter by Msx3 could be relieved by treating transfected cells with trichostatin A, an inhibitor of HDAC(s). Finally, we show that Msx3 and HDAC1 can be co-immunoprecipitated in a complex that does not contain CBP and that Msx3 and HDAC1 proteins are co-localized in the nucleus. Taken together, our results strongly suggest that two distinct multiprotein complexes are present within the nuclei of C2C12 cells: one containing Msx3 and HDAC(s) and another containing Msx3 and CBP and/or p300. On the basis of these results, we propose a dual mechanism of repression by Msx3 protein that involves the squelching of the HAT activity of co-activators, CBP and p300, and recruitment of HDAC(s).

scholarly journals Cellular retinoic acid binding protein 2 inhibits osteogenic differentiation by modulating LIMK1 in C2C12 cells

2015 ◽  
Vol 57 (8) ◽  
pp. 581-589 ◽  
Author(s):  
Rui Wang ◽  
Qingyuan Yang ◽  
Weifan Xiao ◽  
Ruirui Si ◽  
Fenyong Sun ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Osteogenic Differentiation ◽  
Binding Protein ◽  
C2c12 Cells ◽  
Acid Binding Protein

scholarly journals A Novel Muscle-Specific β1 Integrin Binding Protein (Mibp) That Modulates Myogenic Differentiation

1999 ◽  
Vol 147 (7) ◽  
pp. 1391-1398 ◽  
Author(s):  
Ji Li ◽  
Richard Mayne ◽  
Chuanyue Wu
Keyword(s):  
Cell Adhesion ◽  
Myogenic Differentiation ◽  
Binding Protein ◽  
Terminal Differentiation ◽  
C2c12 Cells ◽  
Β1 Integrin ◽  
Adhesion Receptors ◽  
C2c12 Myogenic Cells

Myogenesis is regulated by cell adhesion receptors, including integrins of the β1 family. We report the identification of a novel muscle-specific β1 integrin binding protein (MIBP). MIBP binds to the membrane-proximal cytoplasmic region shared by β1A and β1D integrins, and the binding occurs in vivo as well as in vitro. Furthermore, we show that MIBP is abundantly expressed by C2C12 myogenic cells before fusion, and the expression of MIBP is dramatically downregulated during subsequent differentiation. Finally, we show that overexpression of MIBP in C2C12 cells resulted in a suppression of fusion and terminal differentiation, suggesting that MIBP may play a key role in controlling the progression of muscle differentiation.

scholarly journals YTH-RNA-binding protein prevents deleterious expression of meiotic proteins by tethering their mRNAs to nuclear foci

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Yuichi Shichino ◽  
Yoko Otsubo ◽  
Yoshitaka Kimori ◽  
Masayuki Yamamoto ◽  
Akira Yamashita
Keyword(s):  
Germ Cells ◽  
Target Genes ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Rna Degradation ◽  
Facultative Heterochromatin ◽  
Nuclear Retention ◽  
Nuclear Exosome ◽  
Nuclear Foci

Accurate and extensive regulation of meiotic gene expression is crucial to distinguish germ cells from somatic cells. In the fission yeast Schizosaccharomyces pombe, a YTH family RNA-binding protein, Mmi1, directs the nuclear exosome-mediated elimination of meiotic transcripts during vegetative proliferation. Mmi1 also induces the formation of facultative heterochromatin at a subset of its target genes. Here, we show that Mmi1 prevents the mistimed expression of meiotic proteins by tethering their mRNAs to the nuclear foci. Mmi1 interacts with itself with the assistance of a homolog of Enhancer of Rudimentary, Erh1. Mmi1 self-interaction is required for foci formation, target transcript elimination, their nuclear retention, and protein expression inhibition. We propose that nuclear foci formed by Mmi1 are not only the site of RNA degradation, but also of sequestration of meiotic transcripts from the translation machinery.

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