Interaction Between Methyl CpG-Binding Protein and Ran GTPase during Cell Division in Tobacco Cultured Cells

Yano, Aiko; Kodama, Yutaka; Koike, Akifumi; Shinya, Tomotaka; Kim, Hyun-Jung; Matsumoto, Makoto; Ogita, Shinjiro; Wada, Yuko; Ohad, Nir; Sano, Hiroshi

doi:10.1093/aob/mcl211

Cited by 34 publications

(22 citation statements)

References 25 publications

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“…By contrast, plant RanGAP1 lacks the C-terminal SUMOylation domain, and anchoring of plant RanGAP to the nuclear envelope is mediated by an N-terminal plant-speciWc WPP domain (Jeong et al 2005) and Arabidopsis WPP-domain interacting proteins (WIPs, . Although it has been proven by BiFC assay that AtRan3 is targeted into the nucleus similar to its animal counterpart (Yano et al 2006), AtRan2 localizes to the perinuclear region and nuclear envelope, and is absent inside the nucleus . Arabidopsis UVR8 is structurally similar to the human RCC1 protein that exchanges GDP to GTP for the nuclear small GTP-binding protein Ran (Kliebenstein et al 2002).…”

Section: Introductionmentioning

confidence: 96%

“…The Arabidopsis ortholog of exportin 5, HASTY, which controls phase changes and plant morphology, is located at the periphery of the nucleus and interacts with AtRan1, and presumably regulates nucleocytoplasmic transport of molecules involved in several diVerent morphogenetic pathways (Bollman et al 2003). AtRan3 interacts with a Methyl CpG-binding protein, AtMDB5, and it was proposed that AtRan3 localizes AtMDB5 to the vicinity of chromosomes to maintain the chromatin structure and control chromosome migration during mitosis (Yano et al 2006). Overexpression of plant Ran GTPase suppresses cell cycle defects in Wssion yeast cells carrying a temperaturesensitive pim1 (yeast homologue of mammalian RCC1, a Ran nucleotide exchange factor) mutation (Merkle et al 1994).…”

Section: Introductionmentioning

confidence: 99%

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Phytochrome-mediated differential gene expression of plant Ran/TC4 small G-proteins

Lee

Kim

et al. 2008

Planta

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Ran/TC4 is the only known member of the family of small GTP-binding proteins primarily localized inside the nucleus. We cloned a pea Ran gene (PsRan1) and characterized its expression in tissues, and under different light sources. PsRan1 is a member of a highly homologous multigene family, and it encodes a protein containing plant-specific amino acids in its sequence. It is ubiquitously expressed in pea tissues with high expression in radicles. The amount of total mRNA transcripts representing multiple Ran family members increased in response to very low-fluence R, while the amount of mRNA transcript encoding PsRan1 specifically was not affected by various light treatments. In addition, Ran genes in Arabidopsis were also differentially expressed in various mutants defective in phytochromes or the light-responding HY5 protein, such as phyA, phyB, and hy5. AtRan1 and AtRan3 gene expression was significantly reduced in the phyA mutant background compared to that in Ler-0 wild type plants. AtRan1 expression was also decreased in the phyB background. In contrast, the expression of AtRan2 did not vary in the hy5 and phytochrome mutant backgrounds examined. Interestingly, expression of AtRan1 was significantly reduced in hy5 plants, while AtRan3 expression was increased in the same plants. From these results, we conclude that Ran gene expression is differentially regulated by various light sources and phytochrome-mediated signaling pathways.

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Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Phytochrome-mediated differential gene expression of plant Ran/TC4 small G-proteins

Lee

Kim

et al. 2008

Planta

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“…The binding of the two fusion proteins leads to the reconstitution of the GFP variant, which then produces fluorescence. This technique has been used to successfully dissect interactions between cytokine receptors, cytochromes and transcription factors (Aparicio et al, 2006;Citovsky et al, 2006;Shyu et al, 2006;Yano et al, 2006;Dong et al, 2007) In this study, we used the mouse ortholog of the CD99 gene and BiFC analysis. The results indicate that mCD99 dimerization occurs in the cellular context.…”

Section: Introductionmentioning

confidence: 99%

Detection of homodimer formation of CD99 through extracelluar domain using bimolecular fluorescence complementation analysis

Choi

Lee²,

Jung³

et al. 2007

Exp Mol Med

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Although various functions of CD99 have been reported, such as apoptosis and homotypic aggregation of thymocyte and transendothelial migration of immune cells, biochemical/molecular natures of CD99 are still elusive. Using mouse CD99 gene, we show that CD99 forms homodimer through its extracellular domain. Expression of mouse CD99 is up-regulated on T cells after CD3-mediated activation, like the case for human CD99. The potential of CD99 to form homodimer was tested with a recently developed bimoleular fluorescence complementation analysis (BiFC). In BiFC analysis, the dimerization-induced fluorescence was strong near the perinuclear region and was faded at the cell membrane. However, surface expression of CD99 was still detected by flow cytometry, suggesting that CD99 either in monomer form or in association with other molecules exists on the cell surface. In BiFC analysis using CD99 mutants with its extracellular, transmembrane, or cytosolic domains changed to corresponding human CD4 domains, the mutant replaced with human CD4-extracellular domain did not produce fluorescence. Purified soluble CD99-Fc fusion proteins bound to CD99-Fc immobilized onto the gold sensor chip in surface plasmon resonance analysis, confirming that the extracellular domain was responsible for dimer formation. Intracytoplasmic staining for CD99 expression in the thymocytes and mature T cells showed that most of the cells, even the cells with low surface level of CD99, contained the molecule inside the cell. Our results suggest that majority of CD99 homodimers may exit in the cell and be exported to the cell surface, dissociating from each other, after a certain regulatory signal is delivered.

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“…Ran itself is highly conserved in plants and other species (Ach and Gruissem 1994;Merkle et al 1994;Haizel et al 1997). As in animals, green fluorescence protein (GFP)-tagged Ran localizes to nuclei in tobacco cells (Yano et al 2006). Overexpression of Ran in rice increases the proportion of cells in G2 phase (Wang et al 2006), indicating that Ran is involved in cell cycle progression.…”

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confidence: 99%

Mechanisms of plant spindle formation

Zhang

Dawe

2011

Chromosome Res

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In eukaryotes, the formation of a bipolar spindle is necessary for the equal segregation of chromosomes to daughter cells. Chromosomes, microtubules and kinetochores all contribute to spindle morphogenesis and have important roles during mitosis. A unique property of flowering plant cells is that they entirely lack centrosomes, which in animals have a major role in spindle formation. The absence of these important structures suggests that plants have evolved novel mechanisms to assure chromosome segregation. In this review, we highlight some of the recent studies on plant mitosis and argue that plants utilize a variation of "spindle self-organization" that takes advantage of the early polarity of plant cells and accentuates the role of kinetochores in stabilizing the spindle midzone in prometaphase.

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Interaction Between Methyl CpG-Binding Protein and Ran GTPase during Cell Division in Tobacco Cultured Cells

Cited by 34 publications

References 25 publications

Phytochrome-mediated differential gene expression of plant Ran/TC4 small G-proteins

Phytochrome-mediated differential gene expression of plant Ran/TC4 small G-proteins

Detection of homodimer formation of CD99 through extracelluar domain using bimolecular fluorescence complementation analysis

Mechanisms of plant spindle formation

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