Involvement of the Mouse Prp19 Gene in Neuronal/Astroglial Cell Fate Decisions

Urano, Yumiko; Iiduka, Masayuki; Sugiyama, Akinori; Akiyama, Hirotada; Uzawa, Kouji; Matsumoto, Gaku; Kawasaki, Yasushi; Tashiro, Fumio

doi:10.1074/jbc.m510881200

Cited by 37 publications

(41 citation statements)

References 72 publications

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“…Western blotting (WB) and immunofluorescence analyses were performed as described previously (Urano et al, 2006). For immunoprecipitation analysis, the lysates prepared with lysis buffer containing 1 mM phenylmethylsulfonyl fluoride (PMSF) were incubated with the desired primary antibodies, precipitated with protein A-Sepharose beads (Sigma, St Louis, MO, USA) and analysed by WB.…”

Section: Immunological Analysismentioning

confidence: 99%

“…ChIP and RT-PCR Sheared chromatin from growing or quiescent K2 cells were immunoprecipitated with appropriate antibodies and analysed by PCR (Urano et al, 2006). Then, DNA was extracted and subjected to PCR amplification.…”

Section: Immunological Analysismentioning

confidence: 99%

“…are grateful to Hanum Yaakub and T Sato for their technical assistance. This work was partially supported by the 'Academic Frontier' project for Private Universities: matching fund subsidy from MEXT (Ministry of education, culture, sports, science and technology), 2006 -2010.…”

Section: Acknowledgementsmentioning

confidence: 99%

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Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc

et al. 2007

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Section: Immunological Analysismentioning

confidence: 99%

Section: Immunological Analysismentioning

confidence: 99%

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Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc

et al. 2007

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“…For the immunoprecipitation study, protein extracts were incubated with protein A-Sepharose beads charged with anti-FBI1 antibody or mouse normal serum at 4°C for 3 h. After washing with TNM buffer containing 0.3% Nonidet P-40, proteins were subjected to 12% SDS-PAGE, and Western blotting was performed as described previously (18). Anti-14-3-3␤ (1:800 dilution; Santa Cruz Biotechnology, Inc., Santa Cruz, CA) and anti-FBI1 (1:100) antibodies were used.…”

Section: Methodsmentioning

confidence: 99%

A Novel Binding Factor of 14-3-3β Functions as a Transcriptional Repressor and Promotes Anchorage-independent Growth, Tumorigenicity, and Metastasis

Komiya

Kurabe

Katagiri

et al. 2008

Journal of Biological Chemistry

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107

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The 14-3-3 proteins form a highly conserved family of dimeric proteins that interact with various signal transduction proteins and regulate cell cycle, apoptosis, stress response, and malignant transformation. We previously demonstrated that the ␤ isoform of 14-3-3 proteins promotes tumorigenicity and angiogenesis of rat hepatoma K2 cells. In this study, to analyze the mechanism of 14-3-3␤-induced malignant transformation, yeast two-hybrid screening was performed, and a novel 14-3-3␤-binding factor, FBI1 (fourteen-three-three beta interactant 1), was identified. In vitro binding and co-immunoprecipitation analyses verified specific interaction of 14-3-3␤ with FBI1. The strong expression of FBI1 was observed in several tumor cell lines but not in non-tumor cell lines. Forced expression of antisense FBI1 in K2 cells inhibited anchorage-independent growth but had no significant effect on cell proliferation in monolayer culture. Down-regulation of FBI1 also inhibited tumorigenicity and metastasis accompanying a decrease in MMP-9 (matrix metalloproteinase-9) expression. In addition, the duration of ERK1/2 activation was curtailed in antisense FBI1-expressing K2 cells. A luciferase reporter assay revealed that the FBI1-14-3-3␤ complex could act as a transcriptional silencer, and MKP-1 (MAPK phosphatase-1) was one of the target genes of the FBI1-14-3-3␤ complex. Moreover, chromatin immunoprecipitation analysis demonstrated that FBI1 and 14-3-3␤ were presented on the MKP-1 promoter. These results indicate that FBI1 promotes sustained ERK1/2 activation through repression of MKP-1 transcription, resulting in promotion of tumorigenicity and metastasis.

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“…Very recent findings even indicate that mouse SNEV might be involved in lipid droplet biogenesis (7). Additionally, SNEV seems to play an important role in brain development and function, since it was shown to be gradually downregulated in the hippocampi of patients with Alzheimer's disease (2), and a slightly different splice variant of mouse SNEV might be involved in neuronal/astroglial cell fate decisions (38).…”

mentioning

confidence: 99%

Early Embryonic Lethality of Mice Lacking the Essential Protein SNEV

Fortschegger

Wagner

Voglauer

et al. 2007

Molecular and Cellular Biology

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SNEV (Prp19, Pso4, NMP200) is a nuclear matrix protein known to be involved in pre-mRNA splicing, ubiquitylation, and DNA repair. In human umbilical vein endothelial cells, SNEV overexpression delayed the onset of replicative senescence. Here we analyzed the function of the mouse SNEV gene in vivo by employing homologous recombination in mice and conclude that SNEV is indispensable for early mouse development. Mutant preimplantation embryos initiated blastocyst formation but died shortly thereafter. Outgrowth of SNEV-null blastocysts showed a lack of proliferation of cells of the inner cell mass, which subsequently underwent cell death. While SNEV-heterozygous mice showed no overt phenotype, heterozygous mouse embryonic fibroblast cell lines with reduced SNEV levels displayed a decreased proliferative potential in vitro. Our experiments demonstrate that the SNEV protein is essential, functionally nonredundant, and indispensable for mouse development.SNEV, also known as Prp19, Pso4, or NMP200, is a ubiquitously expressed, highly conserved nuclear matrix protein of 56 kDa and is involved in diverse pathways, such as pre-mRNA splicing (13) and DNA repair (25). Furthermore, SNEV also displays E3 ubiquitin ligase activity in vitro (15, 17). Although it is not an integral part of small nuclear ribonucleoproteins, Prp19 is required for the formation of an activated spliceosomal complex in Saccharomyces cerevisiae (6, 13, 31) by specifying the interaction of U5 and U6 with pre-mRNA (5, 26). The proteins of the Prp19-associated complex (31), which is also called the nineteen complex in yeast or the CDC5L complex in humans (1), and their interactions seem to be conserved in budding and fission yeasts, mammals (20), and even plants (40). Previously we have shown that SNEV is downregulated in senescent human umbilical vein endothelial cells (HUVECs) (14) and that its overexpression leads to an extension of the cellular life span, which correlates with an enhanced stress resistance (39). SNEV is upregulated after exposure to genotoxic agents and seems to be involved in the repair of DNA double-strand breaks and interstrand cross-links (25, 44). Very recent findings even indicate that mouse SNEV might be involved in lipid droplet biogenesis (7). Additionally, SNEV seems to play an important role in brain development and function, since it was shown to be gradually downregulated in the hippocampi of patients with Alzheimer's disease (2), and a slightly different splice variant of mouse SNEV might be involved in neuronal/astroglial cell fate decisions (38).SNEV consists of an N-terminal U-box domain, which is a modified RING finger typical of a new class of ubiquitin E3 ligases (17) that interacts with the proteasome (24), and of seven C-terminal WD40 repeats, which are known to mediate protein-protein interactions (35). The E3 ligase activity might be important for splicing and/or DNA repair by mediating rearrangements through ubiquitylation and degradation of yetunknown targets by the proteasome (24). In between these domains...

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Involvement of the Mouse Prp19 Gene in Neuronal/Astroglial Cell Fate Decisions

Cited by 37 publications

References 72 publications

Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc

Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc

A Novel Binding Factor of 14-3-3β Functions as a Transcriptional Repressor and Promotes Anchorage-independent Growth, Tumorigenicity, and Metastasis

Early Embryonic Lethality of Mice Lacking the Essential Protein SNEV

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