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Your search keyword '"Fujita, Morihisa"' showing total 258 results
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258 results on '"Fujita, Morihisa"'

20. A lipid scramblase TMEM41B is involved in the processing and transport of GPI-anchored proteins.

Author

Cao, Shu-Ya, Liu, Yi-Shi, Gao, Xiao-Dong, Kinoshita, Taroh, and Fujita, Morihisa

Subjects
CARRIER proteins, MEMBRANE proteins, PROTEIN transport, PHOSPHOLIPASE C, LIPIDS, SELENOPROTEINS
Abstract

Protein modification by glycosylphosphatidylinositol (GPI) takes place in the endoplasmic reticulum (ER). GPI-anchored proteins (GPI-APs) formed in the ER are transported to the cell surface through the Golgi apparatus. During transport, the GPI-anchor structure is processed. In most cells, an acyl chain modified to the inositol of GPI is removed by a GPI-inositol deacylase, PGAP1, in the ER. Inositol-deacylated GPI-APs become sensitive to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC). We previously reported that GPI-APs are partially resistant to PI-PLC when PGAP1 activity is weakened by the deletion of selenoprotein T (SELT) or cleft lip and palate transmembrane protein 1 (CLPTM1). In this study, we found that the loss of TMEM41B, an ER-localized lipid scramblase, restored PI-PLC sensitivity of GPI-APs in SELT-knockout (KO) and CLPTM1-KO cells. In TMEM41B-KO cells, the transport of GPI-APs as well as transmembrane proteins from the ER to the Golgi was delayed. Furthermore, the turnover of PGAP1, which is mediated by ER-associated degradation, was slowed in TMEM41B-KO cells. Taken together, these findings indicate that inhibition of TMEM41B-dependent lipid scrambling promotes GPI-AP processing in the ER through PGAP1 stabilization and slowed protein trafficking. [ABSTRACT FROM AUTHOR]

Published
2023
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21. Mitotic phosphorylation inhibits the Golgi mannosidase MAN1A1

Author

Huang, Shijiao, primary, Haga, Yoshimi, additional, Li, Jie, additional, Zhang, Jianchao, additional, Kweon, Hye Kyong, additional, Seino, Junichi, additional, Hirayama, Hiroto, additional, Fujita, Morihisa, additional, Moremen, Kelley W., additional, Andrews, Philip, additional, Suzuki, Tadashi, additional, and Wang, Yanzhuang, additional

Published
2022
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25. Comprehensive proteome and phosphoproteome analysis reveals the protein characterization of invasive ductal and lobular carcinoma with specific molecular subgroup

Author

Yang, Ganglong, primary, Zuo, Chenyang, additional, Fu, Fangmeng, additional, Gao, Xiao-Dong, additional, Lin, Yuxiang, additional, Wen, Piaopiao, additional, Chen, Wenyan, additional, Zhang, Chairui, additional, Xiao, Han, additional, Jiang, Meichen, additional, Zhou, Xiaoman, additional, and Fujita, Morihisa, additional

Published
2022
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26. Genome-wide CRISPR screen reveals CLPTM1L as a lipid scramblase required for efficient glycosylphosphatidylinositol biosynthesis

Author

Wang, Yicheng, primary, Menon, Anant K., additional, Maki, Yuta, additional, Liu, Yi-Shi, additional, Iwasaki, Yugo, additional, Fujita, Morihisa, additional, Guerrero, Paula A., additional, Silva, Daniel Varó’n, additional, Seeberger, Peter H., additional, Murakami, Yoshiko, additional, and Kinoshita, Taroh, additional

Published
2022
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34. GPI Glycan Remodeling by PGAP5 Regulates Transport of GPI-Anchored Proteins from the ER to the Golgi

Author

Fujita, Morihisa, Maeda, Yusuke, Ra, Moonjin, Yamaguchi, Yoshiki, Taguchi, Ryo, and Kinoshita, Taroh

Subjects
Proteins, Universities and colleges, Evolutionary biology, Biological sciences
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2009.08.040 Byline: Morihisa Fujita (1)(5), Yusuke Maeda (1)(2), Moonjin Ra (3), Yoshiki Yamaguchi (4), Ryo Taguchi (3)(5), Taroh Kinoshita (1)(2)(5) Keywords: CELLBIO Abstract: Many eukaryotic proteins are attached to the cell surface via glycosylphosphatidylinositol (GPI) anchors. How GPI-anchored proteins (GPI-APs) are trafficked from the endoplasmic reticulum (ER) to the cell surface is poorly understood, but the GPI moiety has been postulated to function as a signal for sorting and transport. Here, we established mutant cells that were selectively defective in transport of GPI-APs from the ER to the Golgi. We identified a responsible gene, designated PGAP5 (post-GPI-attachment to proteins 5). PGAP5 belongs to a dimetal-containing phosphoesterase family and catalyzed the remodeling of the glycan moiety on GPI-APs. PGAP5 catalytic activity is a prerequisite for the efficient exit of GPI-APs from the ER. Our data demonstrate that GPI glycan acts as an ER-exit signal and suggest that glycan remodeling mediated by PGAP5 regulates GPI-AP transport in the early secretory pathway. Author Affiliation: (1) Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan (2) WPI Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan (3) Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan (4) Structural Glycobiology Team, RIKEN ASI, Saitama 351-0198, Japan (5) Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan Article History: Received 6 March 2009; Revised 29 June 2009; Accepted 12 August 2009 Article Note: (miscellaneous) Published: October 15, 2009

Published
2009

37. Global mapping of glycosylation pathways in human-derived cells

Author

Huang, Yi-Fan, primary, Aoki, Kazuhiro, additional, Akase, Sachiko, additional, Ishihara, Mayumi, additional, Liu, Yi-Shi, additional, Yang, Ganglong, additional, Kizuka, Yasuhiko, additional, Mizumoto, Shuji, additional, Tiemeyer, Michael, additional, Gao, Xiao-Dong, additional, Aoki-Kinoshita, Kiyoko F., additional, and Fujita, Morihisa, additional

Published
2021
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38. PGAP6, a GPI-specific phospholipase A2, has narrow substrate specificity against GPI-anchored proteins

Author

Lee, Gun Hee, 1000030532056, Fujita, Morihisa, Nakanishi, Hideki, 1000050604732, Miyata, Haruhiko, 1000020304066, Ikawa, Masahito, 1000000294124, Maeda, Yusuke, 1000000304048, Murakami, Yoshiko, Kinoshita, Taroh, Lee, Gun Hee, 1000030532056, Fujita, Morihisa, Nakanishi, Hideki, 1000050604732, Miyata, Haruhiko, 1000020304066, Ikawa, Masahito, 1000000294124, Maeda, Yusuke, 1000000304048, Murakami, Yoshiko, and Kinoshita, Taroh

Abstract

Gun-Hee Lee, Morihisa Fujita, Hideki Nakanishi, Haruhiko Miyata, Masahito Ikawa, Yusuke Maeda, Yoshiko Murakami, Taroh Kinoshita, PGAP6, a GPI-specific phospholipase A2, has narrow substrate specificity against GPI-anchored proteins, Journal of Biological Chemistry, Volume 295, Issue 42, 2020, Pages 14501-14509, ISSN 0021-9258, https://doi.org/10.1074/jbc.RA120.014643., PGAP6, also known as TMEM8A, is a phospholipase A2 with specificity to glycosylphosphatidylinositol (GPI) and expressed on the surface of various cells. CRIPTO, a GPI-anchored co-receptor for a morphogenic factor Nodal, is a sensitive substrate of PGAP6. PGAP6-mediated shedding of CRIPTO plays a critical role in an early stage of embryogenesis. In contrast, CRYPTIC, a close family member of CRIPTO, is resistant to PGAP6. In this report, chimeras between CRIPTO and CRYPTIC and truncate mutants of PGAP6 were used to demonstrate that the Cripto-1/FRL1/Cryptic domain of CRIPTO is recognized by an N-terminal domain of PGAP6 for processing. We also report that among 56 human GPI-anchored proteins tested, only glypican 3, prostasin, SPACA4, and contactin-1, in addition to CRIPTO, are sensitive to PGAP6, indicating that PGAP6 has a narrow specificity toward various GPI-anchored proteins.

Published
2020

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