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Article ; Online: Zn

Tsutsumi, Chika / Uegaki, Kaiku / Yamashita, Riyuji / Ushioda, Ryo / Nagata, Kazuhiro

2024 Volume 43, Issue 2, Page(s) 113682

Abstract: ERp18 is an endoplasmic reticulum (ER)-resident thioredoxin (Trx) family protein, similar to cytosolic Trx1. The Trx-like domain occupies a major portion of the whole ERp18 structure, which is postulated to be an ER paralog of cytosolic Trx1. Here, we ... ...

Abstract	ERp18 is an endoplasmic reticulum (ER)-resident thioredoxin (Trx) family protein, similar to cytosolic Trx1. The Trx-like domain occupies a major portion of the whole ERp18 structure, which is postulated to be an ER paralog of cytosolic Trx1. Here, we elucidate that zinc ion (Zn
MeSH term(s)	Animals ; Caenorhabditis elegans ; Hydrogen Peroxide ; Thioredoxins ; Endoplasmic Reticulum ; Zinc
Chemical Substances	Hydrogen Peroxide (BBX060AN9V) ; Thioredoxins (52500-60-4) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2024-02-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.113682
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Article ; Online: Redox states in the endoplasmic reticulum directly regulate the activity of calcium channel, inositol 1,4,5-trisphosphate receptors.

Fujii, Shohei / Ushioda, Ryo / Nagata, Kazuhiro

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 22, Page(s) e2216857120

Abstract: Inositol 1,4,5-trisphosphate receptors (IP3Rs) are one of the two types of tetrameric ion channels that release calcium ion ( ... ...

Abstract	Inositol 1,4,5-trisphosphate receptors (IP3Rs) are one of the two types of tetrameric ion channels that release calcium ion (Ca
MeSH term(s)	Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Calcium/metabolism ; Inositol/metabolism ; Cysteine/metabolism ; Endoplasmic Reticulum/metabolism ; Calcium Signaling/physiology ; Oxidation-Reduction ; Inositol 1,4,5-Trisphosphate/metabolism
Chemical Substances	Inositol 1,4,5-Trisphosphate Receptors ; Calcium (SY7Q814VUP) ; Inositol (4L6452S749) ; Cysteine (K848JZ4886) ; Inositol 1,4,5-Trisphosphate (85166-31-0)
Language	English
Publishing date	2023-05-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2216857120
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Article ; Online: Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis.

Ushioda, Ryo / Nagata, Kazuhiro

Cold Spring Harbor perspectives in biology

2019 Volume 11, Issue 5

Abstract: The endoplasmic reticulum (ER) is a dynamic organelle responsible for many cellular functions in eukaryotic cells. Proper redox conditions in the ER are necessary for the functions of many luminal pathways and the maintenance of homeostasis. The redox ... ...

Abstract	The endoplasmic reticulum (ER) is a dynamic organelle responsible for many cellular functions in eukaryotic cells. Proper redox conditions in the ER are necessary for the functions of many luminal pathways and the maintenance of homeostasis. The redox environment in the ER is oxidative compared with that of the cytosol, and a network of oxidoreductases centering on the protein disulfide isomerase (PDI)-Ero1α hub complex is constructed for efficient electron transfer. Although these oxidizing environments are advantageous for oxidative folding for protein maturation, electron transfer is strictly controlled by Ero1α structurally and spatially. The ER redox environment shifts to a reductive environment under certain stress conditions. In this review, we focus on the reducing reactions that maintain ER homeostasis and introduce their significance in an oxidative ER environment.
MeSH term(s)	Animals ; Endoplasmic Reticulum/physiology ; Gene Expression Regulation/physiology ; Homeostasis/physiology ; Oxidation-Reduction ; Protein Folding
Language	English
Publishing date	2019-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a033910
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Article ; Online: Ca

Yamashita, Riyuji / Fujii, Shohei / Ushioda, Ryo / Nagata, Kazuhiro

Scientific reports

2021 Volume 11, Issue 1, Page(s) 20772

Abstract: The endoplasmic reticulum (ER) is the organelle responsible for the folding of secretory/membrane proteins and acts as a dynamic calcium ion ( ... ...

Abstract	The endoplasmic reticulum (ER) is the organelle responsible for the folding of secretory/membrane proteins and acts as a dynamic calcium ion (Ca
MeSH term(s)	Animals ; Calcium/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation ; HEK293 Cells ; HeLa Cells ; Humans ; Membrane Proteins ; Mice ; Mitochondria/pathology ; Protein Disulfide-Isomerases/genetics ; Protein Disulfide-Isomerases/metabolism
Chemical Substances	Membrane Proteins ; Protein Disulfide-Isomerases (EC 5.3.4.1) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-11-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-99980-9
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Article ; Online: Mechanistic characterization of disulfide bond reduction of an ERAD substrate mediated by cooperation between ERdj5 and BiP.

Cai, Xiaohan / Ito, Shogo / Noi, Kentaro / Inoue, Michio / Ushioda, Ryo / Kato, Yukinari / Nagata, Kazuhiro / Inaba, Kenji

The Journal of biological chemistry

2023 Volume 299, Issue 11, Page(s) 105274

Abstract: Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protein quality control process that eliminates misfolded proteins from the ER. DnaJ homolog subfamily C member 10 (ERdj5) is a protein disulfide isomerase family member that accelerates ERAD ... ...

Abstract	Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protein quality control process that eliminates misfolded proteins from the ER. DnaJ homolog subfamily C member 10 (ERdj5) is a protein disulfide isomerase family member that accelerates ERAD by reducing disulfide bonds of aberrant proteins with the help of an ER-resident chaperone BiP. However, the detailed mechanisms by which ERdj5 acts in concert with BiP are poorly understood. In this study, we reconstituted an in vitro system that monitors ERdj5-mediated reduction of disulfide-linked J-chain oligomers, known to be physiological ERAD substrates. Biochemical analyses using purified proteins revealed that J-chain oligomers were reduced to monomers by ERdj5 in a stepwise manner via trimeric and dimeric intermediates, and BiP synergistically enhanced this action in an ATP-dependent manner. Single-molecule observations of ERdj5-catalyzed J-chain disaggregation using high-speed atomic force microscopy, demonstrated the stochastic release of small J-chain oligomers through repeated actions of ERdj5 on peripheral and flexible regions of large J-chain aggregates. Using systematic mutational analyses, ERAD substrate disaggregation mediated by ERdj5 and BiP was dissected at the molecular level.
MeSH term(s)	Endoplasmic Reticulum Chaperone BiP/chemistry ; Endoplasmic Reticulum Chaperone BiP/genetics ; Endoplasmic Reticulum Chaperone BiP/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Folding ; HEK293 Cells ; Immunoglobulin J-Chains/metabolism ; Protein Domains
Chemical Substances	Endoplasmic Reticulum Chaperone BiP ; Molecular Chaperones ; DNAJC10 protein, human ; Immunoglobulin J-Chains
Language	English
Publishing date	2023-09-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105274
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Article ; Online: The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER.

Uegaki, Kaiku / Tokunaga, Yuji / Inoue, Michio / Takashima, Seiji / Inaba, Kenji / Takeuchi, Koh / Ushioda, Ryo / Nagata, Kazuhiro

Cell reports

2023 Volume 42, Issue 7, Page(s) 112742

Abstract: The endoplasmic reticulum (ER) maintains an oxidative redox environment that is advantageous for the oxidative folding of nascent polypeptides entering the ER. Reductive reactions within the ER are also crucial for maintaining ER homeostasis. However, ... ...

Abstract	The endoplasmic reticulum (ER) maintains an oxidative redox environment that is advantageous for the oxidative folding of nascent polypeptides entering the ER. Reductive reactions within the ER are also crucial for maintaining ER homeostasis. However, the mechanism by which electrons are supplied for the reductase activity within the ER remains unknown. Here, we identify ER oxidoreductin-1α (Ero1α) as an electron donor for ERdj5, an ER-resident disulfide reductase. During oxidative folding, Ero1α catalyzes disulfide formation in nascent polypeptides through protein disulfide isomerase (PDI) and then transfers the electrons to molecular oxygen via flavin adenine dinucleotide (FAD), ultimately yielding hydrogen peroxide (H
MeSH term(s)	Electrons ; Hydrogen Peroxide/metabolism ; Membrane Glycoproteins/metabolism ; Oxidation-Reduction ; Oxidoreductases/metabolism ; Protein Disulfide-Isomerases/metabolism ; Endoplasmic Reticulum/metabolism ; Peptides/metabolism ; Disulfides/metabolism ; Oxidative Stress ; Protein Folding
Chemical Substances	Hydrogen Peroxide (BBX060AN9V) ; Membrane Glycoproteins ; Oxidoreductases (EC 1.-) ; Protein Disulfide-Isomerases (EC 5.3.4.1) ; Peptides ; Disulfides
Language	English
Publishing date	2023-07-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112742
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Article ; Online: Development of a stable antibody production system utilizing an Hspa5 promoter in CHO cells.

Tanemura, Hiroki / Masuda, Kenji / Okumura, Takeshi / Takagi, Eri / Kajihara, Daisuke / Kakihara, Hirofumi / Nonaka, Koichi / Ushioda, Ryo

Scientific reports

2022 Volume 12, Issue 1, Page(s) 7239

Abstract: Chinese hamster ovary (CHO) cells are widely used for manufacturing antibody drugs. We attempted to clone a novel high-expression promoter for producing monoclonal antibodies (mAbs) based on transcriptome analysis to enhance the transcriptional abundance ...

Abstract	Chinese hamster ovary (CHO) cells are widely used for manufacturing antibody drugs. We attempted to clone a novel high-expression promoter for producing monoclonal antibodies (mAbs) based on transcriptome analysis to enhance the transcriptional abundance of mAb genes. The efficacy of conventional promoters such as CMV and hEF1α decrease in the latter phase of fed-batch cell culture. To overcome this, we screened genes whose expression was maintained or increased throughout the culture period. Since CHO cells have diverse genetic expression depending on the selected clone and culture medium, transcriptome analysis was performed on multiple clones and culture media anticipated to be used in mAb manufacturing. We thus acquired the Hspa5 promoter as a novel high-expression promoter, which uniquely enables mAb productivity per cell to improve late in the culture period. Productivity also improved for various IgG subclasses under Hspa5 promoter control, indicating this promoter's potential universal value for mAb production. Finally, it was suggested that mAb production with this promoter is correlated with the transcription levels of endoplasmic reticulum stress-related genes. Therefore, mAb production utilizing the Hspa5 promoter might be a new method for maintaining protein homeostasis and achieving stable expression of introduced mAb genes during fed-batch culture.
MeSH term(s)	Animals ; Antibodies, Monoclonal/genetics ; Antibody Formation ; Batch Cell Culture Techniques ; CHO Cells ; Cricetinae ; Cricetulus ; Culture Media
Chemical Substances	Antibodies, Monoclonal ; Culture Media
Language	English
Publishing date	2022-05-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-11342-1
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Article ; Online: Tolerable glycometabolic stress boosts cancer cell resilience through altered N-glycosylation and Notch signaling activation.

Iwamoto, Shungo / Kobayashi, Takashi / Hanamatsu, Hisatoshi / Yokota, Ikuko / Teranishi, Yukiko / Iwamoto, Akiho / Kitagawa, Miyu / Ashida, Sawako / Sakurai, Ayane / Matsuo, Suguru / Myokan, Yuma / Sugimoto, Aiyu / Ushioda, Ryo / Nagata, Kazuhiro / Gotoh, Noriko / Nakajima, Kazuki / Nishikaze, Takashi / Furukawa, Jun-Ichi / Itano, Naoki

Cell death & disease

2024 Volume 15, Issue 1, Page(s) 53

Abstract: Chronic metabolic stress paradoxically elicits pro-tumorigenic signals that facilitate cancer stem cell (CSC) development. Therefore, elucidating the metabolic sensing and signaling mechanisms governing cancer cell stemness can provide insights into ... ...

Abstract	Chronic metabolic stress paradoxically elicits pro-tumorigenic signals that facilitate cancer stem cell (CSC) development. Therefore, elucidating the metabolic sensing and signaling mechanisms governing cancer cell stemness can provide insights into ameliorating cancer relapse and therapeutic resistance. Here, we provide convincing evidence that chronic metabolic stress triggered by hyaluronan production augments CSC-like traits and chemoresistance by partially impairing nucleotide sugar metabolism, dolichol lipid-linked oligosaccharide (LLO) biosynthesis and N-glycan assembly. Notably, preconditioning with either low-dose tunicamycin or 2-deoxy-D-glucose, which partially interferes with LLO biosynthesis, reproduced the promoting effects of hyaluronan production on CSCs. Multi-omics revealed characteristic changes in N-glycan profiles and Notch signaling activation in cancer cells exposed to mild glycometabolic stress. Restoration of N-glycan assembly with glucosamine and mannose supplementation and Notch signaling blockade attenuated CSC-like properties and further enhanced the therapeutic efficacy of cisplatin. Therefore, our findings uncover a novel mechanism by which tolerable glycometabolic stress boosts cancer cell resilience through altered N-glycosylation and Notch signaling activation.
MeSH term(s)	Humans ; Glycosylation ; Hyaluronic Acid/metabolism ; Resilience, Psychological ; Neoplasm Recurrence, Local/metabolism ; Polysaccharides/metabolism ; Dietary Supplements ; Neoplastic Stem Cells/metabolism
Chemical Substances	Hyaluronic Acid (9004-61-9) ; Polysaccharides
Language	English
Publishing date	2024-01-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-024-06432-z
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Article ; Online: The endoplasmic reticulum-associated degradation and disulfide reductase ERdj5.

Ushioda, Ryo / Nagata, Kazuhiro

Methods in enzymology

2011 Volume 490, Page(s) 235–258

Abstract: The endoplasmic reticulum (ER) is an organelle where secretory or membrane proteins are correctly folded with the aid of various molecular chaperones and oxidoreductases. Only correctly folded and assembled proteins are enabled to reach their final ... ...

Abstract	The endoplasmic reticulum (ER) is an organelle where secretory or membrane proteins are correctly folded with the aid of various molecular chaperones and oxidoreductases. Only correctly folded and assembled proteins are enabled to reach their final destinations, which are called as ER quality control (ERQC) mechanisms. ER-associated degradation (ERAD) is one of the ERQC mechanisms for maintaining the ER homeostasis and facilitates the elimination of misfolded or malfolded proteins accumulated in the ER. ERAD is mainly consisting of three processes: recognition of misfolded proteins for degradation in the ER, retrotranslocation of (possibly) unfolded substrates from the ER to the cytosol through dislocation channel, and their degradation in the cytosol via ubiquitin-protesome system. After briefly mentioned on productive folding of nascent polypeptides in the ER, we here overview the above three processes in ERAD system by highlighting on novel ERAD factors such as EDEM and ERdj5 in mammals and yeasts.
MeSH term(s)	Animals ; Disulfides/metabolism ; Endoplasmic Reticulum/enzymology ; Endoplasmic Reticulum/physiology ; Glycosylation ; HSP40 Heat-Shock Proteins/genetics ; HSP40 Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Folding ; Proteins/chemistry ; Proteins/metabolism ; Stress, Physiological/physiology ; Ubiquitin/metabolism ; Unfolded Protein Response/physiology
Chemical Substances	DNAJC10 protein, human ; Disulfides ; HSP40 Heat-Shock Proteins ; Molecular Chaperones ; Proteins ; Ubiquitin
Language	English
Publishing date	2011
Publishing country	United States
Document type	Journal Article
ISSN	1557-7988 ; 0076-6879
ISSN (online)	1557-7988
ISSN	0076-6879
DOI	10.1016/B978-0-12-385114-7.00014-3
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Article ; Online: Glycosylation-independent ERAD pathway serves as a backup system under ER stress.

Ushioda, Ryo / Hoseki, Jun / Nagata, Kazuhiro

Molecular biology of the cell

2013 Volume 24, Issue 20, Page(s) 3155–3163

Abstract: During endoplasmic reticulum (ER)-associated degradation (ERAD), terminally misfolded proteins are retrotranslocated from the ER to the cytosol and degraded by the ubiquitin-proteasome system. Misfolded glycoproteins are recognized by calnexin and ... ...

Abstract	During endoplasmic reticulum (ER)-associated degradation (ERAD), terminally misfolded proteins are retrotranslocated from the ER to the cytosol and degraded by the ubiquitin-proteasome system. Misfolded glycoproteins are recognized by calnexin and transferred to EDEM1, followed by the ER disulfide reductase ERdj5 and the BiP complex. The mechanisms involved in ERAD of nonglycoproteins, however, are poorly understood. Here we show that nonglycoprotein substrates are captured by BiP and then transferred to ERdj5 without going through the calnexin/EDEM1 pathway; after cleavage of disulfide bonds by ERdj5, the nonglycoproteins are transferred to the ERAD scaffold protein SEL1L by the aid of BiP for dislocation into the cytosol. When glucose trimming of the N-glycan groups of the substrates is inhibited, glycoproteins are also targeted to the nonglycoprotein ERAD pathway. These results indicate that two distinct pathways for ERAD of glycoproteins and nonglycoproteins exist in mammalian cells, and these pathways are interchangeable under ER stress conditions.
MeSH term(s)	Animals ; Calnexin/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/genetics ; Endoplasmic Reticulum Stress/physiology ; Endoplasmic Reticulum-Associated Degradation/genetics ; Endoplasmic Reticulum-Associated Degradation/physiology ; Glucose/metabolism ; Glycosylation ; HEK293 Cells ; HeLa Cells ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Proteasome Endopeptidase Complex/metabolism ; Protein Folding ; Proteolysis ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Edem1 protein, mouse ; Membrane Proteins ; Calnexin (139873-08-8) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2013-08-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E13-03-0138
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