Search

Your search keyword '"Okumura, Masaki"' showing total 383 results
Start Over Author "Okumura, Masaki"
383 results on '"Okumura, Masaki"'

3. Insights into Land Plant Evolution Garnered from the Marchantia polymorpha Genome

Author

Bowman, John L, Kohchi, Takayuki, Yamato, Katsuyuki T, Jenkins, Jerry, Shu, Shengqiang, Ishizaki, Kimitsune, Yamaoka, Shohei, Nishihama, Ryuichi, Nakamura, Yasukazu, Berger, Frédéric, Adam, Catherine, Aki, Shiori Sugamata, Althoff, Felix, Araki, Takashi, Arteaga-Vazquez, Mario A, Balasubrmanian, Sureshkumar, Barry, Kerrie, Bauer, Diane, Boehm, Christian R, Briginshaw, Liam, Caballero-Perez, Juan, Catarino, Bruno, Chen, Feng, Chiyoda, Shota, Chovatia, Mansi, Davies, Kevin M, Delmans, Mihails, Demura, Taku, Dierschke, Tom, Dolan, Liam, Dorantes-Acosta, Ana E, Eklund, D Magnus, Florent, Stevie N, Flores-Sandoval, Eduardo, Fujiyama, Asao, Fukuzawa, Hideya, Galik, Bence, Grimanelli, Daniel, Grimwood, Jane, Grossniklaus, Ueli, Hamada, Takahiro, Haseloff, Jim, Hetherington, Alexander J, Higo, Asuka, Hirakawa, Yuki, Hundley, Hope N, Ikeda, Yoko, Inoue, Keisuke, Inoue, Shin-ichiro, Ishida, Sakiko, Jia, Qidong, Kakita, Mitsuru, Kanazawa, Takehiko, Kawai, Yosuke, Kawashima, Tomokazu, Kennedy, Megan, Kinose, Keita, Kinoshita, Toshinori, Kohara, Yuji, Koide, Eri, Komatsu, Kenji, Kopischke, Sarah, Kubo, Minoru, Kyozuka, Junko, Lagercrantz, Ulf, Lin, Shih-Shun, Lindquist, Erika, Lipzen, Anna M, Lu, Chia-Wei, De Luna, Efraín, Martienssen, Robert A, Minamino, Naoki, Mizutani, Masaharu, Mizutani, Miya, Mochizuki, Nobuyoshi, Monte, Isabel, Mosher, Rebecca, Nagasaki, Hideki, Nakagami, Hirofumi, Naramoto, Satoshi, Nishitani, Kazuhiko, Ohtani, Misato, Okamoto, Takashi, Okumura, Masaki, Phillips, Jeremy, Pollak, Bernardo, Reinders, Anke, Rövekamp, Moritz, Sano, Ryosuke, Sawa, Shinichiro, Schmid, Marc W, Shirakawa, Makoto, Solano, Roberto, Spunde, Alexander, Suetsugu, Noriyuki, Sugano, Sumio, Sugiyama, Akifumi, Sun, Rui, Suzuki, Yutaka, and Takenaka, Mizuki

Subjects
Biological Sciences, Genetics, Life on Land, Adaptation, Biological, Biological Evolution, Embryophyta, Gene Expression Regulation, Plant, Genome, Plant, Marchantia, Molecular Sequence Annotation, Signal Transduction, Transcription, Genetic, Marchantia polymorpha, auxin, charophycean algae, land plant evolution, sex chromosome, Medical and Health Sciences, Developmental Biology, Biological sciences, Biomedical and clinical sciences
Abstract

The evolution of land flora transformed the terrestrial environment. Land plants evolved from an ancestral charophycean alga from which they inherited developmental, biochemical, and cell biological attributes. Additional biochemical and physiological adaptations to land, and a life cycle with an alternation between multicellular haploid and diploid generations that facilitated efficient dispersal of desiccation tolerant spores, evolved in the ancestral land plant. We analyzed the genome of the liverwort Marchantia polymorpha, a member of a basal land plant lineage. Relative to charophycean algae, land plant genomes are characterized by genes encoding novel biochemical pathways, new phytohormone signaling pathways (notably auxin), expanded repertoires of signaling pathways, and increased diversity in some transcription factor families. Compared with other sequenced land plants, M. polymorpha exhibits low genetic redundancy in most regulatory pathways, with this portion of its genome resembling that predicted for the ancestral land plant. PAPERCLIP.

Published
2017

4. Boosting the enzymatic activity of CxxC motif-containing PDI family members.

Author

Kuramochi, Tsubura, Yamashita, Yukino, Arai, Kenta, Kanemura, Shingo, Muraoka, Takahiro, and Okumura, Masaki

Subjects
PROTEIN disulfide isomerase, SULFHYDRYL group, THIOLS, GLUTATHIONE
Abstract

Compounds harboring high acidity and oxidizability of thiol groups permit tuning the redox equilibrium constants of CxxC sites of members of the protein disulphide isomerase (PDI) family and thus can be used to accelerate folding processes and increase the production of native proteins by minimal loading in comparison to glutathione. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

6. Zinc finger domains bind low-complexity domain polymers

Author

Iguchi, Naohiko, primary, Isozumi, Noriyoshi, additional, Hattori, Yoshikazu, additional, Imamura, Tomohiro, additional, So, Masatomo, additional, Nanaura, Hitoki, additional, Kiriyama, Takao, additional, Eura, Nobuyuki, additional, Yamaoka, Minako, additional, Nakanishi, Mari, additional, Mori, Masashi, additional, Ohki, Shinya, additional, Kumeta, Hiroyuki, additional, Koga, Hironori, additional, Watabe, Mai, additional, Mabuchi, Takuya, additional, Kanemura, Shingo, additional, Okumura, Masaki, additional, Yoshizawa, Takuya, additional, Ota, Ichiro, additional, Suzuki, Naoki, additional, Aoki, Masashi, additional, Yamashiro, Yoshito, additional, Saio, Tomohide, additional, Sugie, Kazuma, additional, and Mori, Eiichiro, additional

Published
2023
Full Text
View/download PDF

8. Dose-response relationship for the resistance of human insulin to degradation by insulin-degrading enzyme

Author

Okumura, Masaki, primary, Kuramochi, Tsubura, additional, Lin, Yuxi, additional, Furukawa, Ran, additional, Mizutani, Kenji, additional, Yokoyama, Takeshi, additional, Kim, Mingeun, additional, Lim, Mi Hee, additional, Yi, Hyon-Seung, additional, Arai, Kenta, additional, Yamaguchi, Hiroshi, additional, Hojo, Hironobu, additional, Iwaoka, Michio, additional, Tanaka, Yoshikazu, additional, Park, Sam-Yong, additional, Inaba, Kenji, additional, Kanemura, Shingo, additional, and Lee, Young-Ho, additional

Published
2023
Full Text
View/download PDF

20. A tonoplast‐localized magnesium transporter is crucial for stomatal opening in Arabidopsis under high Mg2+ conditions

Author

Inoue, Shin‐ichiro, Hayashi, Maki, Huang, Sheng, Yokosho, Kengo, Gotoh, Eiji, Ikematsu, Shuka, Okumura, Masaki, Suzuki, Takamasa, Kamura, Takumi, Kinoshita, Toshinori, Ma, Jian Feng, Inoue, Shin‐ichiro, Hayashi, Maki, Huang, Sheng, Yokosho, Kengo, Gotoh, Eiji, Ikematsu, Shuka, Okumura, Masaki, Suzuki, Takamasa, Kamura, Takumi, Kinoshita, Toshinori, and Ma, Jian Feng

Abstract

Plant stomata play an important role in CO2 uptake for photosynthesis and transpiration, but the mechanisms underlying stomatal opening and closing under changing environmental conditions are still not completely understood. Through large-scale genetic screening, we isolated an Arabidopsis mutant (closed stomata2 (cst2)) that is defective in stomatal opening. We cloned the causal gene (MGR1/CST2) and functionally characterized this gene. The mutant phenotype was caused by a mutation in a gene encoding an unknown protein with similarities to the human magnesium (Mg2+) efflux transporter ACDP/CNNM. MGR1/CST2 was localized to the tonoplast and showed transport activity for Mg2+. This protein was constitutively and highly expressed in guard cells. Knockout of this gene resulted in stomatal closing, decreased photosynthesis and growth retardation, especially under high Mg2+ conditions, while overexpression of this gene increased stomatal opening and tolerance to high Mg2+ concentrations. Furthermore, guard cell-specific expression of MGR1/CST2 in the mutant partially restored its stomatal opening. Our results indicate that MGR1/CST2 expression in the leaf guard cells plays an important role in maintaining cytosolic Mg2+ concentrations through sequestering Mg2+ into vacuoles, which is required for stomatal opening, especially under high Mg2+ conditions.

Published
2022

21. Is prolongation of corrected QT interval associated with seizures induced by electroconvulsive therapy reduced by atropine sulfate?

Author

Suzuki, Yoko, Miyajima, Miho, Ohta, Katsuya, Yoshida, Noriko, Omoya, Rie, Fujiwara, Mayo, Watanabe, Takafumi, Okumura, Masaki, Yamazaki, Hiroaki, Shintaku, Masayuki, Murata, Issei, Ozaki, Shigeru, Sasaki, Takeshi, Nakamura, Mitsuru, Suwa, Hiroshi, Sasano, Tetsuo, Kawara, Tokuhiro, Matsuura, Masato, and Matsushima, Eisuke

Published
2017
Full Text
View/download PDF

27. A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization

Author

Okumura, Masaki, primary, Kanemura, Shingo, additional, Matsusaki, Motonori, additional, Kinoshita, Misaki, additional, Saio, Tomohide, additional, Ito, Dai, additional, Hirayama, Chihiro, additional, Kumeta, Hiroyuki, additional, Watabe, Mai, additional, Amagai, Yuta, additional, Lee, Young-Ho, additional, Akiyama, Shuji, additional, and Inaba, Kenji, additional

Published
2021
Full Text
View/download PDF

28. Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding

Author

Matsusaki, Motonori, primary, Okada, Rina, additional, Tanikawa, Yuya, additional, Kanemura, Shingo, additional, Ito, Dai, additional, Lin, Yuxi, additional, Watabe, Mai, additional, Yamaguchi, Hiroshi, additional, Saio, Tomohide, additional, Lee, Young-Ho, additional, Inaba, Kenji, additional, and Okumura, Masaki, additional

Published
2021
Full Text
View/download PDF

33. A tonoplast‐localized magnesium transporter is crucial for stomatal opening in Arabidopsis under high Mg2+ conditions.

Author

Inoue, Shin‐ichiro, Hayashi, Maki, Huang, Sheng, Yokosho, Kengo, Gotoh, Eiji, Ikematsu, Shuka, Okumura, Masaki, Suzuki, Takamasa, Kamura, Takumi, Kinoshita, Toshinori, and Ma, Jian Feng

Subjects
STOMATA, GROWTH disorders, MAGNESIUM, GENETIC overexpression, GENETIC testing, ARABIDOPSIS, PLANT transpiration
Abstract

Summary: Plant stomata play an important role in CO2 uptake for photosynthesis and transpiration, but the mechanisms underlying stomatal opening and closing under changing environmental conditions are still not completely understood.Through large‐scale genetic screening, we isolated an Arabidopsis mutant (closed stomata2 (cst2)) that is defective in stomatal opening. We cloned the causal gene (MGR1/CST2) and functionally characterized this gene.The mutant phenotype was caused by a mutation in a gene encoding an unknown protein with similarities to the human magnesium (Mg2+) efflux transporter ACDP/CNNM. MGR1/CST2 was localized to the tonoplast and showed transport activity for Mg2+. This protein was constitutively and highly expressed in guard cells. Knockout of this gene resulted in stomatal closing, decreased photosynthesis and growth retardation, especially under high Mg2+ conditions, while overexpression of this gene increased stomatal opening and tolerance to high Mg2+ concentrations. Furthermore, guard cell‐specific expression of MGR1/CST2 in the mutant partially restored its stomatal opening.Our results indicate that MGR1/CST2 expression in the leaf guard cells plays an important role in maintaining cytosolic Mg2+ concentrations through sequestering Mg2+ into vacuoles, which is required for stomatal opening, especially under high Mg2+ conditions. [ABSTRACT FROM AUTHOR]

Published
2022
Full Text
View/download PDF

35. Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding

Author

Matsusaki, Motonori, Okada, Rina, Tanikawa, Yuya, Kanemura, Shingo, Ito, Dai, Lin, Yuxi, Watabe, Mai, Yamaguchi, Hiroshi, Saio, Tomohide, Lee, Young-Ho, Inaba, Kenji, Okumura, Masaki, Matsusaki, Motonori, Okada, Rina, Tanikawa, Yuya, Kanemura, Shingo, Ito, Dai, Lin, Yuxi, Watabe, Mai, Yamaguchi, Hiroshi, Saio, Tomohide, Lee, Young-Ho, Inaba, Kenji, and Okumura, Masaki

Abstract

The physiological functions of proteins are destined by their unique three-dimensional structures. Almost all biological kingdoms share conserved disulfide-catalysts and chaperone networks that assist in correct protein folding and prevent aggregation. Disruption of these networks is implicated in pathogenesis, including neurodegenerative disease. In the mammalian endoplasmic reticulum (ER), more than 20 members of the protein disulfide isomerase family (PDIs) are believed to cooperate in the client folding pathway, but it remains unclear whether complex formation among PDIs via non-covalent interaction is involved in regulating their enzymatic and chaperone functions. Herein, we report novel functional hetero complexes between PDIs that promote oxidative folding and inhibit aggregation along client folding. The findings provide insight into the physiological significance of disulfide-catalyst and chaperone networks and clues for understanding pathogenesis associated with disruption of the networks., P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfide bonds in cultured cells, but it remains unclear whether complex formation between P5 and other PDIs is involved in regulating enzymatic and chaperone functions. Herein, we established the far-western blot method to detect non-covalent interactions between P5 and other PDIs and found that PDI and ERp72 are partner proteins of P5. The enzymatic activity of P5-mediated oxidative folding is up-regulated by PDI, while the chaperone activity of P5 is stimulated by ERp72. These findings shed light on the mechanism by which the complex formations among PDIs drive to synergistically accelerate protein folding and prevents aggregation. This knowledge has implications for understanding misfolding-related pathology.

Published
2021

36. Ca2+ Regulates ERp57-Calnexin Complex Formation

Author

Tanikawa, Yuya, Kanemura, Shingo, Ito, Dai, Lin, Yuxi, Matsusaki, Motonori, Kuroki, Kimiko, Yamaguchi, Hiroshi, Maenaka, Katsumi, Lee, Young-Ho, Inaba, Kenji, Okumura, Masaki, Tanikawa, Yuya, Kanemura, Shingo, Ito, Dai, Lin, Yuxi, Matsusaki, Motonori, Kuroki, Kimiko, Yamaguchi, Hiroshi, Maenaka, Katsumi, Lee, Young-Ho, Inaba, Kenji, and Okumura, Masaki

Abstract

ERp57, a member of the protein disulfide isomerase family, is a ubiquitous disulfide catalyst that functions in the oxidative folding of various clients in the mammalian endoplasmic reticulum (ER). In concert with ER lectin-like chaperones calnexin and calreticulin (CNX/CRT), ERp57 functions in virtually all folding stages from co-translation to post-translation, and thus plays a critical role in maintaining protein homeostasis, with direct implication for pathology. Here, we present mechanisms by which Ca2+ regulates the formation of the ERp57-calnexin complex. Biochemical and isothermal titration calorimetry analyses revealed that ERp57 strongly interacts with CNX via a non-covalent bond in the absence of Ca2+. The ERp57-CNX complex not only promoted the oxidative folding of human leukocyte antigen heavy chains, but also inhibited client aggregation. These results suggest that this complex performs both enzymatic and chaperoning functions under abnormal physiological conditions, such as Ca2+ depletion, to effectively guide proper oxidative protein folding. The findings shed light on the molecular mechanisms underpinning crosstalk between the chaperone network and Ca2+.

Published
2021

43. Ca2+ Regulates ERp57-Calnexin Complex Formation

Author

Tanikawa, Yuya, primary, Kanemura, Shingo, additional, Ito, Dai, additional, Lin, Yuxi, additional, Matsusaki, Motonori, additional, Kuroki, Kimiko, additional, Yamaguchi, Hiroshi, additional, Maenaka, Katsumi, additional, Lee, Young-Ho, additional, Inaba, Kenji, additional, and Okumura, Masaki, additional

Published
2021
Full Text
View/download PDF

44. CIPK23 regulates blue light-dependent stomatal opening in Arabidopsis thaliana

Author

Inoue, Shin‐Ichiro, Kaiserli, Eirini, Zhao, Xiang, Waksman, Thomas, Takemiya, Atsushi, Okumura, Masaki, Takahashi, Hirotaka, Seki, Motoaki, Shinozaki, Kazuo, Endo, Yaeta, Sawasaki, Tatsuya, Kinoshita, Toshinori, Zhang, Xiao, Christie, John M., and Shimazaki, Ken‐Ichiro

Subjects
animal structures
Abstract

Phototropins (phot1 and phot2) are plant blue light receptor kinases that function to mediate phototropism, chloroplast movement, leaf flattening, and stomatal opening in Arabidopsis. Considerable progress has been made in understanding the mechanisms associated with phototropin receptor activation by light. However, the identities of phototropin signaling components are less well understood by comparison. In this study, we specifically searched for protein kinases that interact with phototropins by using an in vitro screening method (AlphaScreen) to profile interactions against an Arabidopsis protein kinase library. We found that CBL‐interacting protein kinase 23 (CIPK23) interacts with both phot1 and phot2. Although these interactions were verified by in vitro pull‐down and in vivo bimolecular fluorescence complementation assays, CIPK23 was not phosphorylated by phot1, as least in vitro. Mutants lacking CIPK23 were found to exhibit impaired stomatal opening in response to blue light but no deficits in other phototropin‐mediated responses. We further found that blue light activation of inward‐rectifying K+ (K+in) channels was impaired in the guard cells of cipk23 mutants, whereas activation of the plasma membrane H+‐ATPase was not. The blue light activation of K+in channels was also impaired in the mutant of BLUS1, which is one of the phototropin substrates in guard cells. We therefore conclude that CIPK23 promotes stomatal opening through activation of K+in channels most likely in concert with BLUS1, but through a mechanism other than activation of the H+‐ATPase. The role of CIPK23 as a newly identified component of phototropin signaling in stomatal guard cells is discussed.

Published
2020

45. Antipsychotic olanzapine-induced misfolding of proinsulin in the endoplasmic reticulum accounts for atypical development of diabetes

Author

30439244, 70182194, Ninagawa, Satoshi, Tada, Seiichiro, Okumura, Masaki, Inoguchi, Kenta, Kinoshita, Misaki, Kanemura, Shingo, Imami, Koshi, Umezawa, Hajime, Ishikawa, Tokiro, Mackin, Robert B, Torii, Seiji, Ishihama, Yasushi, Inaba, Kenji, Anazawa, Takayuki, Nagamine, Takahiko, Mori, Kazutoshi, 30439244, 70182194, Ninagawa, Satoshi, Tada, Seiichiro, Okumura, Masaki, Inoguchi, Kenta, Kinoshita, Misaki, Kanemura, Shingo, Imami, Koshi, Umezawa, Hajime, Ishikawa, Tokiro, Mackin, Robert B, Torii, Seiji, Ishihama, Yasushi, Inaba, Kenji, Anazawa, Takayuki, Nagamine, Takahiko, and Mori, Kazutoshi

Published
2020

Catalog

Books, media, physical & digital resources
See catalog results