Regulation of in vitro nucleic acid strand annealing activity of heterogeneous nuclear ribonucleoprotein protein A1 by reversible phosphorylation

Idriss, Haitham T.; Kumar, Arun; Casas‐Finet, José R.; Guo, Hong; Damuni, Zahi; Wilson, Samuel H.

doi:10.1021/bi00203a037

Cited by 51 publications

(34 citation statements)

References 48 publications

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“…However, it is also possible that such Ca 2ϩ -binding factors may directly or indirectly regulate IRES activity in response to changes in cytosolic Ca 2ϩ levels. Indeed, the IRES-trans acting factors (ITAFs) hnRNP A and hnRNP C are known to bind calmodulin in the presence of Ca 2ϩ (44) and in addition, hnRNP A is also known to be regulated by PKC phosphorylation which alters its ability to bind RNA (45,46). Thus, these data potentially link Ca 2ϩ signaling pathways to ITAF activity.…”

Section: Discussionmentioning

confidence: 98%

Protein Kinase C Regulates Internal Initiation of Translation of the GATA-4 mRNA following Vasopressin-induced Hypertrophy of Cardiac Myocytes

Sharma

Masri

et al. 2007

Journal of Biological Chemistry

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GATA-4 is a key member of the GATA family of transcription factors involved in cardiac development and growth as well as in cardiac hypertrophy and heart failure. Our previous studies suggest that GATA-4 protein synthesis may be translationally regulated. We report here that the 518-nt long 5-untranslated region (5-UTR) of the GATA-4 mRNA, which is predicted to form stable secondary structures (؊65 kcal/mol) such as to be inhibitory to cap-dependent initiation, confers efficient translation to monocistronic reporter mRNAs in cell-free extracts. Moreover, uncapped GATA-4 5-UTR containing monocistronic reporter mRNAs continue to be well translated while capped reporters are insensitive to the inhibition of initiation by cap-analog, suggesting a capindependent mechanism of initiation. Utilizing a dicistronic luciferase mRNA reporter containing the GATA-4 5-UTR within the intercistronic region, we demonstrate that this leader sequence confers functional internal ribosome entry site (IRES) activity. The activity of the GATA-4 IRES is unaffected in trans-differentiating P19CL6 cells, however, is strongly stimulated immediately following arginine-vasopressin exposure of H9c2 ventricular myocytes. IRES activity is then maintained at submaximal levels during hypertrophic growth of these cells. Supraphysiological Ca 2؉ levels diminished stimulation of IRES activity immediately following exposure to vasopressin and inhibition of protein kinase C activity utilizing a pseudosubstrate peptide sequence blocked IRES activity during hypertrophy. Thus, our data suggest a mechanism for GATA-4 protein synthesis under conditions of reduced global cap-dependent translation, which is maintained at a submaximal level during hypertrophic growth and point to the regulation of GATA-4 IRES activity by sarco(ER)-reticular Ca 2؉ stores and PKC.

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Section: Discussionmentioning

confidence: 98%

Protein Kinase C Regulates Internal Initiation of Translation of the GATA-4 mRNA following Vasopressin-induced Hypertrophy of Cardiac Myocytes

Sharma

Masri

et al. 2007

Journal of Biological Chemistry

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“…HnRNP proteins are also regulated by phosphorylation (8,21,29). Phosphorylation of LR1 is required for binding to DNA target sequences, but the kinase that mediates LR1 phosphorylation is currently unknown.…”

Section: Discussionmentioning

confidence: 99%

Regulation of the Epstein-Barr Virus C Promoter by AUF1 and the Cyclic AMP/Protein Kinase A Signaling Pathway

Fuentes‐Pananá

Peng

Brewer

et al. 2000

J Virol

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EBNA2 is an Epstein-Barr virus (EBV)-encoded protein that regulates the expression of viral and cellular genes required for EBV-driven B-cell immortalization.Elucidating the mechanisms by which EBNA2 regulates viral and cellular gene expression is necessary to understand EBV-induced B-cell immortalization and viral latency in humans. EBNA2 targets to the latency C promoter (Cp) through an interaction with the cellular DNA binding protein CBF1 (RBPJk). The EBNA2 enhancer in Cp also binds another cellular factor, C promoter binding factor 2 (CBF2), whose protein product(s) has not yet been identified. Within the EBNA2 enhancer in Cp, we have previously identified the DNA sequence required for CBF2 binding and also determined that this element is required for efficient activation of Cp by EBNA2. In this study, the CBF2 activity was biochemically purified and microsequenced. The peptides sequenced were identical to the hnRNP protein AUF1. Antibodies against AUF1 but not antibodies to related hnRNP proteins reacted with CBF2 in gel mobility shift assays. In addition, stimulation of the cellular cyclic AMP (cAMP)/protein kinase A (PKA) signal transduction pathway results in an increase in detectable CBF2/AUF1 binding activity extracted from stimulated cells. Furthermore, the CBF2 binding site was able to confer EBNA2 responsiveness to a heterologous promoter when transfected cells were treated with compounds that activate PKA or by cotransfection of plasmids expressing a constitutively active catalytic subunit of PKA. EBNA2-mediated stimulation of the latency Cp is also increased in similar cotransfection assays. These results further support an important role for CBF2 in mediating EBNA2 transactivation; they identify the hnRNP protein AUF1 as a major component of CBF2 and are also the first evidence of a cis-acting sequence other than a CBF1 binding element that is able to confer responsiveness to EBNA2.

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“…Although stimulation of these signalling pathways markedly increased reporter gene expression in cells expressing GAL4-hnRNP D0 (Table 1), stimulation increased reporter gene expression of control samples as well. Protein kinase C, protein kinase A and casein kinase II phosphorylate hnRNP A1 in itro, and it has been shown that its phosphorylation state affects its ability to interact with RNA [34,35]. hnRNP A2 is also phosphorylated by casein kinase II [36].…”

Section: Discussionmentioning

confidence: 99%

Heterogeneous nuclear ribonucleoprotein D0 contains transactivator and DNA-binding domains

Tolnay

Baranyi

Tsokos

2000

Biochemical Journal

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Heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) is an abundant, ubiquitous protein that binds RNA and DNA sequences specifically, and has been implicated in the transcriptional regulation of the human complement receptor 2 gene. We found that in i o expression of hnRNP D0-GAL4 fusion proteins increased the transcriptional activity of a GAL4-driven reporter gene, providing direct proof that hnRNP D0 possesses a transactivator domain. We found, using truncated hnRNP D0 proteins fused to GAL4, that 29 amino acids in the N-terminal region are critical for transactivation. We established, using a series of recombinant truncated hnRNP D0 proteins, that the tandem RNA-binding domains alone were not able to bind double-stranded DNA. Nevertheless, 24 additional amino acids of the C-terminus imparted sequence-specific DNA binding.

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Regulation of in vitro nucleic acid strand annealing activity of heterogeneous nuclear ribonucleoprotein protein A1 by reversible phosphorylation

Cited by 51 publications

References 48 publications

Protein Kinase C Regulates Internal Initiation of Translation of the GATA-4 mRNA following Vasopressin-induced Hypertrophy of Cardiac Myocytes

Protein Kinase C Regulates Internal Initiation of Translation of the GATA-4 mRNA following Vasopressin-induced Hypertrophy of Cardiac Myocytes

Regulation of the Epstein-Barr Virus C Promoter by AUF1 and the Cyclic AMP/Protein Kinase A Signaling Pathway

Heterogeneous nuclear ribonucleoprotein D0 contains transactivator and DNA-binding domains

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