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Your search keyword '"Miura, Masayuki"' showing total 844 results
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844 results on '"Miura, Masayuki"'

154. HIF-1α-PDK1 axis-induced active glycolysis plays an essential role in macrophage migratory capacity

Author

Semba, Hiroaki, primary, Takeda, Norihiko, additional, Isagawa, Takayuki, additional, Sugiura, Yuki, additional, Honda, Kurara, additional, Wake, Masaki, additional, Miyazawa, Hidenobu, additional, Yamaguchi, Yoshifumi, additional, Miura, Masayuki, additional, Jenkins, Dana M. R., additional, Choi, Hyunsung, additional, Kim, Jung-whan, additional, Asagiri, Masataka, additional, Cowburn, Andrew S., additional, Abe, Hajime, additional, Soma, Katsura, additional, Koyama, Katsuhiro, additional, Katoh, Manami, additional, Sayama, Keimon, additional, Goda, Nobuhito, additional, Johnson, Randall S., additional, Manabe, Ichiro, additional, Nagai, Ryozo, additional, and Komuro, Issei, additional

Published
2016
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157. A STRIPAK component Strip regulates neuronal morphogenesis by affecting microtubule stability

Author

Sakuma, Chisako, Okmura, Misako, Umehara, Tomoki, Miura, Masayuki, Chihara, Takahiro, Sakuma, Chisako, Okmura, Misako, Umehara, Tomoki, Miura, Masayuki, and Chihara, Takahiro

Abstract

During neural development, regulation of microtubule stability is essential for proper morphogenesis of neurons. Recently, the striatin-interacting phosphatase and kinase (STRIPAK) complex was revealed to be involved in diverse cellular processes. However, there is little evidence that STRIPAK components regulate microtubule dynamics, especially in vivo. Here, we show that one of the core STRIPAK components, Strip, is required for microtubule organization during neuronal morphogenesis. Knockdown of Strip causes a decrease in the level of acetylated α-tubulin in Drosophila S2 cells, suggesting that Strip influences the stability of microtubules. We also found that Strip physically and genetically interacts with tubulin folding cofactor D (TBCD), an essential regulator of α- and β-tubulin heterodimers. Furthermore, we demonstrate the genetic interaction between strip and Down syndrome cell adhesion molecule (Dscam), a cell surface molecule that is known to work with TBCD. Thus, we propose that Strip regulates neuronal morphogenesis by affecting microtubule stability., This work was supported by grants from the Japanese Ministry of Education, Science, Sports, Culture and Technology (MEXT), the Japan Society for the Promotion of Science and the Japan Science and Technology Agency (to C.S., M.O., M.M. and T.C.).

Published
2015

160. Red‐Shifted Fluorogenic Substrate for Detection of lacZ‐Positive Cells in Living Tissue with Single‐Cell Resolution.

Author

Ito, Hiroki, Kawamata, Yu, Kamiya, Mako, Tsuda‐Sakurai, Kayoko, Tanaka, Shinji, Ueno, Tasuku, Komatsu, Toru, Hanaoka, Kenjiro, Okabe, Shigeo, Miura, Masayuki, and Urano, Yasuteru

Subjects
SUBSTRATES (Materials science), FLUORESCENCE, ESCHERICHIA coli, GALACTOSIDASES, GREEN fluorescent protein
Abstract

The Escherichia coli lacZ gene encoding β‐galactosidase is a widely used reporter, but few synthetic substrates are available for detecting its activity with single‐cell resolution in living samples. Our recently reported fluorogenic substrate SPiDER‐βGal is suitable for this purpose, but its hydrolysis product shows green fluorescence emission, and a red‐shifted analogue is therefore required for use in combination with green fluorescent protein (GFP) markers. Herein, we describe the development of a red‐shifted fluorogenic substrate for β‐galactosidase, SPiDER‐Red‐βGal, based on a silicon rhodol scaffold and a carboxylic group as the intramolecular nucleophile. LacZ‐positive cells were successfully labeled with SPiDER‐Red‐βGal at single‐cell resolution in living samples, which enabled us to visualize different cell types in combination with GFP markers. SPiDER and the fly: A new fluorogenic β‐galactosidase substrate, SPiDER‐Red‐βGal, based on a silicon rhodol scaffold and a carboxylic group as the intramolecular nucleophile, exhibited simultaneous activation of red fluorescence and labeling ability for intracellular proteins via a quinone methide intermediate. The probe can label lacZ‐positive cells at single‐cell resolution in vivo with perfect orthogonality to green fluorescent protein (GFP) markers. [ABSTRACT FROM AUTHOR]

Published
2018
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165. Drosophila Strip serves as a platform for early endosome organization during axon elongation

Author

Sakuma, Chisako, Kawauchi, Takeshi, Haraguchi, Shuka, Shikanai, Mima, Yamaguchi, Yoshifumi, Gelfand, Vladimir I, Luo, Liqun, Miura, Masayuki, Chihara, Takahiro, Sakuma, Chisako, Kawauchi, Takeshi, Haraguchi, Shuka, Shikanai, Mima, Yamaguchi, Yoshifumi, Gelfand, Vladimir I, Luo, Liqun, Miura, Masayuki, and Chihara, Takahiro

Abstract

type:text, Early endosomes are essential for regulating cell signalling and controlling the amount of cell surface molecules during neuronal morphogenesis. Early endosomes undergo retrograde transport (clustering) before their homotypic fusion. Small GTPase Rab5 is known to promote early endosomal fusion, but the mechanism linking the transport/clustering with Rab5 activity is unclear. Here we show that Drosophila Strip is a key regulator for neuronal morphogenesis. Strip knockdown disturbs the early endosome clustering, and Rab5-positive early endosomes become smaller and scattered. Strip genetically and biochemically interacts with both Glued (the regulator of dynein-dependent transport) and Sprint (the guanine nucleotide exchange factor for Rab5), suggesting that Strip is a molecular linker between retrograde transport and Rab5 activation. Overexpression of an active form of Rab5 in strip-mutant neurons suppresses the axon elongation defects. Thus, Strip acts as a molecular platform for the early endosome organization that has important roles in neuronal morphogenesis., This work was supported by grants from the National Institute of General Medical Science of the National Institutes of Health (R01-GM085232 to V.I.G.), the National Institutes of Health (R01-DC005982 to L.L.), the Japanese Ministry of Education, Science, Sports, Culture, and Technology (MEXT), the Japan Society for the Promotion of Science, and the Japan Science and Technology Agency (to C.S., K.T., Y.Y., M.M., and T.C.).

Published
2014

169. Single-Cell Imaging of Caspase-1 Dynamics Reveals an All-or-None Inflammasome Signaling Response

Author

Liu, Ting, primary, Yamaguchi, Yoshifumi, additional, Shirasaki, Yoshitaka, additional, Shikada, Koichi, additional, Yamagishi, Mai, additional, Hoshino, Katsuaki, additional, Kaisho, Tsuneyasu, additional, Takemoto, Kiwamu, additional, Suzuki, Toshihiko, additional, Kuranaga, Erina, additional, Ohara, Osamu, additional, and Miura, Masayuki, additional

Published
2014
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175. 1P306 Analysis of non-classical secretion of IL-1β using real-time single-cell secretion imaging(27. Bioimaging,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

Author

Shirasaki, Yoshitaka, primary, Liu, Ting, additional, Yamaguchi, Yoshifumi, additional, Yamaguchi, Mai, additional, Suzuki, Nobutake, additional, Izawa, Kazushi, additional, Mizuno, Jun, additional, Shoji, Shuichi, additional, Harada, Yoshie, additional, Nishikomori, Ryuta, additional, Heike, Toshio, additional, Miura, Masayuki, additional, and Ohara, Osamu, additional

Published
2014
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177. Local Apoptosis Modulates Early Mammalian Brain Development through the Elimination of Morphogen-Producing Cells

Author

Nonomura, Keiko, primary, Yamaguchi, Yoshifumi, additional, Hamachi, Misato, additional, Koike, Masato, additional, Uchiyama, Yasuo, additional, Nakazato, Kenichi, additional, Mochizuki, Atsushi, additional, Sakaue-Sawano, Asako, additional, Miyawaki, Atsushi, additional, Yoshida, Hiroki, additional, Kuida, Keisuke, additional, and Miura, Masayuki, additional

Published
2013
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178. The Kelch Repeat Protein KLHDC10 Regulates Oxidative Stress-Induced ASK1 Activation by Suppressing PP5

Author

Sekine, Yusuke, Hatanaka, Ryo, Watanabe, Takeshi, Sono, Naoki, Iemura, Shun-ichiro, Natsume, Tohru, Kuranaga, Erina, Miura, Masayuki, Takeda, Kohsuke, Ichijo, Hidenori, Sekine, Yusuke, Hatanaka, Ryo, Watanabe, Takeshi, Sono, Naoki, Iemura, Shun-ichiro, Natsume, Tohru, Kuranaga, Erina, Miura, Masayuki, Takeda, Kohsuke, and Ichijo, Hidenori

Abstract

Reactive oxygen species (ROS)-induced activation of Apoptosis signal-regulating kinase 1 (ASK1) plays crucial roles in oxidative stress-mediated cell death through the activation of the JNK and p38 MAPK pathways. However, the regulatory mechanism of ASK1 in the oxidative stress response remains to be elucidated. Here, we identified the kelch repeat protein, Slim, as an activator of ASK1 through a Drosophila misexpression screen. We also performed a proteomics screen and revealed that Kelch domain containing 10 (KLHDC10), a mammalian ortholog of Slim, interacted with Protein phosphatase 5 (PP5), which has been shown to inactivate ASK1 in response to ROS. KLHDC10 bound to the phosphatase domain of PP5 and suppressed its phosphatase activity. Moreover, KLHDC10 was required for H2O2-induced sustained activation of ASK1 and cell death in Neuro2A cells. These findings suggest that Slim/KLHDC10 is an activator of ASK1, contributing to oxidative stress-induced cell death through the suppression of PP5.

Published
2012

182. Detection of LacZ-Positive Cells in Living Tissue with Single-Cell Resolution.

Author

Doura, Tomohiro, Kamiya, Mako, Obata, Fumiaki, Yamaguchi, Yoshifumi, Hiyama, Takeshi Y., Matsuda, Takashi, Fukamizu, Akiyoshi, Noda, Masaharu, Miura, Masayuki, and Urano, Yasuteru

Subjects
TISSUES, SINGLE cell proteins, ESCHERICHIA coli, GALACTOSIDASES, NEURONS
Abstract

The LacZ gene, which encodes Escherichia coli β-galactosidase, is widely used as a marker for cells with targeted gene expression or disruption. However, it has been difficult to detect lacZ-positive cells in living organisms or tissues at single-cell resolution, limiting the utility of existing lacZ reporters. Herein we present a newly developed fluorogenic β-galactosidase substrate suitable for labeling live cells in culture, as well as in living tissues. This precisely functionalized fluorescent probe exhibited dramatic activation of fluorescence upon reaction with the enzyme, remained inside cells by anchoring itself to intracellular proteins, and provided single-cell resolution. Neurons labeled with this probe preserved spontaneous firing, which was enhanced by application of ligands of receptors expressed in the cells, suggesting that this probe would be applicable to investigate functions of targeted cells in living tissues and organisms. [ABSTRACT FROM AUTHOR]

Published
2016
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