Molecular properties and intracellular localization of rat liver nuclear scaffold protein P130

Hibino, Yasuhide; Usui, Tatsuhiro; Morita, Yasuhiro; Hirose, Noriko; Okazaki, Mari; Sugano, Nobuhiko; Hiraga, Kenji

doi:10.1016/j.bbaexp.2006.04.010

Cited by 48 publications

(77 citation statements)

References 74 publications

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“…Our previous report described the principal properties of matrin 3 [3]. First, matrin 3 has several functionally confirmed motifs including NLS, NES, ZF1, ZF2, RB1, RB2, and MRS. Second, matrin 3 is localized not only in the nuclear scaffold but also in the soluble fraction in the nucleus, and in the cytoplasmic, microsomal and polysomal fractions of rat liver cells.…”

Section: Discussionmentioning

confidence: 99%

“…In our previous work, a 4.6-kb long P130 cDNA (AB205483) was cloned to determine the molecular properties of P130 [3]. P130, comprising 845 amino acid residues and having molecular mass of 95.3 kDa, was identical in structure to rat matrin 3 (BC062231) as revised from that published by Belgrader et al [4], and highly similar to human and mouse matrin 3 (BC015031 and BC090833, respectively).…”

Section: Introductionmentioning

confidence: 99%

“…cDNA encoding wild-type or deletion mutants of matrin 3 were prepared by ligating the PCR-amplified product and subcloning into pcDNA [3]. Plasmid DNA was propagated in E. coli DH5α and the final preparation was obtained by CsCl equilibrium centrifugation.…”

Section: Cell Linementioning

confidence: 99%

“…EMSA was performed using the [ 32 P] Xmn I fragment with nuclear extract in a final volume of 25 µl of reaction mixture containing 10 mM Tris-HCl (pH 7.4), 40 mM NaCl, 1 mM EDTA, 4% glycerol, and 1 mM 2-mercaptoethanol. Nuclear extracts were prepared from Ac2F and Ac2F highly expressing matrin 3 [3]. In brief, all the mixtures were incubated at room temperature for 30 min.…”

Section: Preparation Of the 32 P-labeled Xmn I Fragment And Electrophmentioning

confidence: 99%

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Matrin 3 Augments the Transcriptional Activity of an SV40 Promoter-Mediated Luciferase Gene with a Highly Repetitive DNA Component

Kamiuchi¹,

Fukaya²,

Usui³

et al. 2014

J Mol Genet Med

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We examined the transcriptional augmentation of matrin 3, a nuclear matrix protein, of the SV40 promotermediated luciferase gene (pGL3) following transient transfection of recombinant plasmids into cells. It has been reported that the interaction of the Xmn I fragment, a highly repetitive DNA component as one of a typical matrix-or scaffold-attachment regions (MAR/SAR) tethered upstream from the SV40 promoter (pGL3-Xmn I) with matrin 3 appeared to be required for augmentation of luciferase gene transcription. In this study, we investigated the levels of induction in cells overexpressing the wild type and several deletion mutants of matrin 3. It appeared that pGL3-Xmn I augmented luciferase production to 4-times the control level in Ac2F cells, but 23-fold in cells overexpressing matrin 3. Electrophoretic mobility shift assay showed that the Xmn I fragment augmented luciferase gene transcription through interaction with matrin 3. Furthermore, our findings suggest that all of the functional domains tested in matrin 3 were necessary for transcriptional augmentation. We aim not only to describe the transcriptional augmentation of matrin 3 with MAR/SAR, but also to strengthen interest in their use to mediate the expression of therapeutic transgenes.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Cell Linementioning

confidence: 99%

Section: Preparation Of the 32 P-labeled Xmn I Fragment And Electrophmentioning

confidence: 99%

See 2 more Smart Citations

Matrin 3 Augments the Transcriptional Activity of an SV40 Promoter-Mediated Luciferase Gene with a Highly Repetitive DNA Component

Kamiuchi¹,

Fukaya²,

Usui³

et al. 2014

J Mol Genet Med

View full text Add to dashboard Cite

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“…3B, bottom). In addition to a major 125-kDa species, additional matrin 3 forms were detected: these are suspected to reflect additional modified and/or phosphorylated forms of matrin 3, as seen in other studies (29). The specificities of the matrin 3 species and the antibodies used in its detection were established using a blocking peptide for the matrin 3 antibodies, which efficiently blocked anti-matrin 3 from binding matrin 3 in immunoprecipitates (Fig.…”

Section: Methodsmentioning

confidence: 99%

The Alphaherpesvirus US3/ORF66 Protein Kinases Direct Phosphorylation of the Nuclear Matrix Protein Matrin 3

Erazo

Yee

Banfield

et al. 2011

J Virol

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The protein kinase found in the short region of alphaherpesviruses, termed US3 in herpes simplex virus type 1 (HSV-1) and pseudorabies virus (PRV) and ORF66 in varicella-zoster virus (VZV), affects several viral and host cell processes, and its specific targets remain an area of active investigation. Reports suggesting that HSV-1 US3 substrates overlap with those of cellular protein kinase A (PKA) prompted the use of an antibody specific for phosphorylated PKA substrates to identify US3/ORF66 targets. HSV-1, VZV, and PRV induced very different substrate profiles that were US3/ORF66 kinase dependent. The predominant VZV-phosphorylated 125-kDa species was identified as matrin 3, one of the major nuclear matrix proteins. Matrin 3 was also phosphorylated by HSV-1 and PRV in a US3 kinase-dependent manner and by VZV ORF66 kinase at a novel residue (KRRRT150EE). Since VZV-directed T150 phosphorylation was not blocked by PKA inhibitors and was not induced by PKA activation, and since PKA predominantly targeted matrin 3 S188, it was concluded that phosphorylation by VZV was PKA independent. However, purified VZV ORF66 kinase did not phosphorylate matrin 3 in vitro, suggesting that additional cellular factors were required. In VZV-infected cells in the absence of the ORF66 kinase, matrin 3 displayed intranuclear changes, while matrin 3 showed a pronounced cytoplasmic distribution in late-stage cells infected with US3-negative HSV-1 or PRV. This work identifies phosphorylation of the nuclear matrix protein matrin 3 as a new conserved target of this kinase group.All herpesviruses studied to date encode proteins predicted to be protein kinases, based on the presence of conserved signature domains common to cellular kinases. Considerable interest in their roles and functions has developed, because they influence multiple cellular processes by controlling the phosphorylation of both cellular and viral proteins. Two serine/ threonine (S/T)-specific protein kinases are found in alphaherpesvirus genomes: the UL13 kinase of herpes simplex virus types 1 and 2 (HSV-1 and HSV-2) (open reading frame 47 [ORF47] in varicella-zoster virus [VZV]) has recognizable homologues in all known herpesviruses, whereas the US3 kinase (ORF66 in VZV) is found in the short genomic region of members of the alphaherpesvirus subfamily. Both alphaherpesvirus kinases are genetically dispensable for viral growth in culture, but kinase-deficient viruses invariably show impaired replication in specific cell types and/or attenuation in animal models of disease (22,37,45,57,62,64,65,73,79), suggesting important roles that are dependent on the host cell environment.The 393-residue ORF66 protein kinase of VZV has such cell-specific importance. VZV causes chickenpox upon primary infection and herpes zoster upon reactivation from a prolonged neuronal latent state. VZVs expressing ORF66 that is translationally halted or kinase inactive show only modest growth impairment in cell cultures used for VZV propagation and in human skin in the SCID-hu mouse model but show s...

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Knockdown of genes involved in axonal transport enhances the toxicity of human neuromuscular disease‐linked MATR3 mutations in Drosophila

et al. 2020

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Mutations in the nuclear matrix protein Matrin 3 (MATR3) have been identified in amyotrophic lateral sclerosis and myopathy. To investigate the mechanisms underlying MATR3 mutations in neuromuscular diseases and efficiently screen for modifiers of MATR3 toxicity, we generated transgenic MATR3 flies. Our findings indicate that expression of wild‐type or mutant MATR3 in motor neurons reduces climbing ability and lifespan of flies, while their expression in indirect flight muscles (IFM) results in abnormal wing positioning and muscle degeneration. In both motor neurons and IFM, mutant MATR3 expression results in more severe phenotypes than wild‐type MATR3, demonstrating that the disease‐linked mutations confer pathogenicity. We conducted a targeted candidate screen for modifiers of the MATR3 abnormal wing phenotype and identified multiple enhancers involved in axonal transport. Knockdown of these genes enhanced protein levels and insolubility of mutant MATR3. These results suggest that accumulation of mutant MATR3 contributes to toxicity and implicate axonal transport dysfunction in disease pathogenesis.

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Molecular properties and intracellular localization of rat liver nuclear scaffold protein P130

Cited by 48 publications

References 74 publications

Matrin 3 Augments the Transcriptional Activity of an SV40 Promoter-Mediated Luciferase Gene with a Highly Repetitive DNA Component

Matrin 3 Augments the Transcriptional Activity of an SV40 Promoter-Mediated Luciferase Gene with a Highly Repetitive DNA Component

The Alphaherpesvirus US3/ORF66 Protein Kinases Direct Phosphorylation of the Nuclear Matrix Protein Matrin 3

Knockdown of genes involved in axonal transport enhances the toxicity of human neuromuscular disease‐linked MATR3 mutations in Drosophila

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