Functional Domains of Template-Activating Factor-I as a Protein Phosphatase 2A Inhibitor

Saito, Shoko; Miyaji-Yamaguchi, Mary; Shimoyama, Tae; Nagata, Kyosuke

doi:10.1006/bbrc.1999.0790

Cited by 72 publications

(82 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Four abundant HeLa cell proteins specifically associate and physically interact with HuR, recognizing the third RRM (RNA recognition motif): SETa, SETb, pp32, and APRIL . All these proteins are inhibitors of protein phosphatase 2A (Li et al, 1996;Saito et al, 1999), which suggests a role in the regulation by HuR .…”

Section: Hurmentioning

confidence: 98%

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Bevilacqua

Ceriani

Capaccioli

et al. 2003

Journal Cellular Physiology

294

259

View full text Add to dashboard Cite

Recent evidence suggests that gene expression may be regulated, at least in part, at post-transcriptional level by factors inducing the extremely rapid degradation of messenger RNAs. These factors include reactions between adenyl-uridyl-rich elements (AREs) of the relevant mRNA and either specific proteins that bind to these elements or exosomes. This review deals with examples of the proteins (AU-rich binding proteins, AUBPs) and exosomes, which have been shown to form complexes with AREs and bring about rapid degradation of the relevant mRNA, and with certain other factors, which protect the RNA from such degradation. The biochemical and physiological factors underlying the stability of messenger RNAs carrying the ARE motifs will be reviewed in the light of their emerging significance for cell physiology, human pathology, and molecular medicine. We also consider the possible application of the results of recent insights into the mechanisms to pharmacological interventions to prevent or cure disorders, especially developmental disorders, which the suppression of gene expression may bring about. Molecular targeting of specific steps in protein degradation by synthetic compounds has already been utilized for the development of pharmacological therapies.

show abstract

Section: Hurmentioning

confidence: 98%

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Bevilacqua

Ceriani

Capaccioli

et al. 2003

Journal Cellular Physiology

294

259

View full text Add to dashboard Cite

show abstract

“…[2][3][4] SET (also known as template-activating factor I beta (TAF-Ib)) physically interacts with several protein complexes, which suggests that it has diverse functions including Granzyme A-induced apoptosis, 5,6 chromosome remodeling, 7 transcriptional regulation, 8 mRNA stabilization 9 and cell cycle regulation. [10][11][12][13] SET also forms a complex with the MLL leukemic fusion protein and type-2A protein phosphatase (PP2A). 14 Among other functions, PP2A regulates cell cycle progression, 15,16 and one target of PP2A is the mitogen-activated protein kinase (MAPK)/ extracellular signal-regulated protein kinase (ERK) pathway.…”

Section: Introductionmentioning

confidence: 99%

“…14 Among other functions, PP2A regulates cell cycle progression, 15,16 and one target of PP2A is the mitogen-activated protein kinase (MAPK)/ extracellular signal-regulated protein kinase (ERK) pathway. 17 SET inhibits PP2A activity, 10,12 and overexpression of SET activates MAPK and prevents Fas-mediated apoptosis. 17 It has been proposed that SET has opposite functions during cell cycle progression: 13,18 First, SET binds p21.…”

Section: Introductionmentioning

confidence: 99%

SET-induced calcium signaling and MAPK/ERK pathway activation mediate dendritic cell-like differentiation of U937 cells

Kandilci

Grosveld

2005

Leukemia

View full text Add to dashboard Cite

Human SET, a target of chromosomal translocation in human leukemia encodes a highly conserved, ubiquitously expressed, nuclear phosphoprotein. SET mediates many functions including chromatin remodeling, transcription, apoptosis and cell cycle control. We report that overexpression of SET directs differentiation of the human promonocytic cell line U937 along the dendritic cell (DC) pathway, as cells display typical morphologic changes associated with DC fate and express the DC surface markers CD11b and CD86. Differentiation occurs via a calcium-dependent mechanism involving the CaMKII and MAPK/ERK pathways. Similar responses are elicited by interferon-c (IFN-c) treatment with the distinction that IFN-c signaling activates the DNA-binding activity of STAT1 whereas SET overexpression does not. In addition, unlike IFN-c signaling, SET generated stress-induced p38/MAPK activity. Interestingly, IFN-c treatment transiently upregulated endogenous SET in a dose-dependent manner. These results suggest that SET is part of both IFN-c-mediated and stress-mediated cellular responses and that SET induces cell differentiation via calcium and MAPK/ ERK pathways.

show abstract

“…Although pools of PP2A are known to reside in the nucleus as well as the cytoplasm (Adachi et al, 1994), we did not detect PP2A subunit peptides by mass spectrometric analysis of GST-WNV C pulldowns. Because capsid binds to the same region of I 2 PP2A that is required for inhibition of PP2A (Saito et al, 1999), it seems likely that the capsid-dependent increase in phosphatase activity results from preventing I2 PP2A from binding to PP2A. As such, the mechanisms by which WNV C and hepatitis C virus NS5A activate PP2A appear to be distinct (Duong et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…PP2A that is essential for interaction with the Cdk5-activating protein p35 (residues 29-94) (Saito et al, 1999;Qu et al, 2002). Binding of I2 PP2A to p35 is associated with activation of the Cdk5 complex that is required for signalling at the neuromuscular synapse (Fu et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I₂^PP2A

Hunt¹,

Urbanowski²,

Kakani³

et al. 2007

Cell Microbiol

View full text Add to dashboard Cite

show abstract

Functional Domains of Template-Activating Factor-I as a Protein Phosphatase 2A Inhibitor

Cited by 72 publications

References 20 publications

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

SET-induced calcium signaling and MAPK/ERK pathway activation mediate dendritic cell-like differentiation of U937 cells

Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I₂^PP2A

Contact Info

Product

Resources

About

Functional Domains of Template-Activating Factor-I as a Protein Phosphatase 2A Inhibitor

Cited by 72 publications

References 20 publications

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

SET-induced calcium signaling and MAPK/ERK pathway activation mediate dendritic cell-like differentiation of U937 cells

Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I2PP2A

Contact Info

Product

Resources

About

Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I₂^PP2A