Involvement of the catalytic subunit of protein kinase A and of HA95 in pre-mRNA splicing

Kvissel, Anne-Katrine; Ørstavik, Sigurd; Eikvar, Sissel; Brede, Gaute; Jahnsen, Tore; Collas, Philippe; Akusjärvi, Göran; Skålhegg, Bjørn Steen

doi:10.1016/j.yexcr.2007.05.014

Cited by 47 publications

(62 citation statements)

References 40 publications

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“…To date, multiple kinases, including SR protein kinase 1 (SRPK1) (36), SRPK2 (37), Cdc-like kinase (Clk/Sty) (38), DNA topoisomerase I (39), cAMP-dependent protein kinase (PKA), and AKT (40,41), have been shown to phosphorylate the RS domain of SF2/ASF. We recently found that Dyrk1A phosphorylates SF2/ASF, SC35, and 9G8 and regulates both subcellular localization and activity (13,14,19).…”

Section: Discussionmentioning

confidence: 99%

Dual-specificity Tyrosine Phosphorylation-regulated Kinase 1A (Dyrk1A) Modulates Serine/Arginine-rich Protein 55 (SRp55)-promoted Tau Exon 10 Inclusion

Yin

Jin

et al. 2012

Journal of Biological Chemistry

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Background: Dysregulation of the alternative splicing of Tau exon 10 causes several types of neurodegenerative diseases. Results: SRp55 promotes Tau exon 10 inclusion. Dyrk1A interacts with SRp55, mainly phosphorylates its proline-rich domain and inhibits its ability to promote Tau exon 10 inclusion. Conclusion: Dyrk1A suppresses SRp55-promoted Tau exon 10 inclusion. Significance: Up-regulation of Dyrk1A disrupts the alternative splicing of Tau exon 10.

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Section: Discussionmentioning

confidence: 99%

Dual-specificity Tyrosine Phosphorylation-regulated Kinase 1A (Dyrk1A) Modulates Serine/Arginine-rich Protein 55 (SRp55)-promoted Tau Exon 10 Inclusion

Yin

Jin

et al. 2012

Journal of Biological Chemistry

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“…SFRS17A Colocalizes with the PKA C Subunit and SC35 in HEK293T Cells-A subpopulation of the PKA C subunit has been shown to be localized to SFCs in the nucleus, where it colocalizes with the splicing factor SC35 (29). Furthermore, SFRS17A and SC35 colocalize in well defined spots (Fig.…”

Section: Resultsmentioning

confidence: 89%

“…It has, in fact, earlier been shown that PKA can phosphorylate the SR protein ASF/SF2 in vitro (47) and the polypyrimidine tract-binding protein in vivo (48). Studies have, however, been conducted that suggest that pre-mRNA splicing is regulated by PKA through a cAMP-independent mechanism (29). The latter finding implies either that the regulation is mediated by free PKA C subunits or that the PKA R 2 C 2 complex would not have to be activated by cAMP and could remain as an intact holoenzyme while regulating this process.…”

Section: Discussionmentioning

confidence: 99%

“…E1A Splicing Assay-E1A splicing assays were performed as described (29). Briefly described, U-2OS cells grown in 6-well dishes were co-transfected with 0.5 g of the splicing reporter minigene E1A and 1.5 g of either C␣, SFRS17A, SFRS17A(L438P/L439P/K445P/K445P), ASF/SF2, or empty pFLAG-CMV-5a plasmid using FuGENE 6 (Roche Applied Science).…”

Section: Methodsmentioning

confidence: 99%

“…Upon activation of the PKA holoenzyme, a part of the C subunit pool enters the nucleus, where it is involved in regulation of transcription and splicing (29). Introns are removed from pre-mRNAs by the spliceosome, a massive complex that consists of five small nuclear ribonucleoprotein particles, U1, U2, U4, U5 and U6, associated with a large number of proteins.…”

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Splicing Factor Arginine/Serine-rich 17A (SFRS17A) Is an A-kinase Anchoring Protein That Targets Protein Kinase A to Splicing Factor Compartments

Jarnæss

Stokka

Kvissel

et al. 2009

Journal of Biological Chemistry

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Protein kinase A (PKA) is targeted to distinct subcellular localizations by specific protein kinase A anchoring proteins (AKAPs). AKAPs are divided into subclasses based on their ability to bind type I or type II PKA or both. Dual-specificity AKAPs were recently reported to have an additional PKA binding determinant called the RI specifier region. A bioinformatic search with the consensus RI specifier region identified a novel AKAP, the splicing factor arginine/serine-rich 17A (SFRS17A). Here, we show by a variety of protein interaction assays that SFRS17A binds both type I and type II PKA in vitro and inside cells, demonstrating that SFRS17A is a dual-specific AKAP. Moreover, immunofluorescence experiments show that SFRS17A colocalizes with the catalytic subunit of PKA as well as the splicing factor SC35 in splicing factor compartments. Using the E1A minigene splicing assay, we found that expression of wild type SFRS17A conferred regulation of E1A alternative splicing, whereas the mutant SFRS17A, which is unable to bind PKA, did not. Our data suggest that SFRS17A is an AKAP involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments.

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Quantitative phosphoproteomics reveals link between Helicobacter pylori infection and RNA splicing modulation in host cells

Holland¹,

Schmid²,

Zimny‐Arndt³

et al. 2011

Proteomics

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The Gram-negative, spiral-shaped bacterium Helicobacter pylori is a common human pathogen that causes chronic inflammation of the human gastric mucosa, leading to peptic ulceration and/or gastric cancer. Here, we analyzed changes in the phosphoproteome of gastric epithelial cells (AGS) upon infection with H. pylori using a combination of SILAC, phosphoprotein enrichment, 2-DE, and MALDI TOF/TOF-MS. From a total of 526 spots we identified 391 protein species (143 proteins) and quantified 332 (127 proteins). Nearly, one-third of the identified proteins (40/143) were associated with the spliceosome or RNA splicing. The abundance of 20 proteins was altered by H. pylori infection, in particular, a number of serine arginine-rich (SR) proteins involved in the regulation and control of alternative splicing. Importantly, the combined methodologies enabled the detection of infection-dependent protein species-specific regulation, suggesting functional modulation of individual protein species. These findings reveal unexpected new insights into the mechanisms of host cell manipulation by H. pylori, which are likely associated with gastric pathologies, including gastric cancer.

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Involvement of the catalytic subunit of protein kinase A and of HA95 in pre-mRNA splicing

Cited by 47 publications

References 40 publications

Dual-specificity Tyrosine Phosphorylation-regulated Kinase 1A (Dyrk1A) Modulates Serine/Arginine-rich Protein 55 (SRp55)-promoted Tau Exon 10 Inclusion

Dual-specificity Tyrosine Phosphorylation-regulated Kinase 1A (Dyrk1A) Modulates Serine/Arginine-rich Protein 55 (SRp55)-promoted Tau Exon 10 Inclusion

Splicing Factor Arginine/Serine-rich 17A (SFRS17A) Is an A-kinase Anchoring Protein That Targets Protein Kinase A to Splicing Factor Compartments

Quantitative phosphoproteomics reveals link between Helicobacter pylori infection and RNA splicing modulation in host cells

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