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

Mechanistic characterization of disulfide bond reduction of an ERAD substrate mediated by cooperation between ERdj5 and BiP

Journal of Biological Chemistry VOLUME 299, ISSUE 11, 105274, NOVEMBER 2023

https://www.jbc.org/article/S0021-9258(23)02302-5/fulltext

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

The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER

Cell Reports Volume 42, Issue 7, 25 July 2023, 112742

https://doi.org/10.1016/j.celrep.2023.112742

Shohei Fujii, Ryo Ushioda and Kazuhiro Nagata

Redox states in the endoplasmic reticulum directly regulate the activity of calcium channel, inositol 1,4,5-trisphosphate receptors

Proceedings of the National Academy of Sciences of the United States of America, May 22 2023, 120 (22) e2216857120

https://www.pnas.org/doi/10.1073/pnas.2216857120

Kondoh, H., & Fujii, M.

Definitive Endoderm from EpiSC Aggregates in Matrigel.

Methods in molecular biology, 2490, 205–212.

https://doi.org/10.1007/978-1-0716-2281-0_15

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

Ca2+ imbalance caused by ERdj5 deletion affects mitochondrial fragmentation

Scientific Reports Volume 11, Article number: 20772 (2021)

https://www.nature.com/articles/s41598-021-99980-9

Zhang K, Bao R, Huang F, Yang K, Ding Y, Lauterboeck L, Yoshida M, Long Q, Yang Q.

ATP synthase inhibitory factor subunit 1 regulates islet β-cell function via repression of mitochondrial homeostasis.

Lab Invest. 2021 Oct 4. doi: 10.1038/s41374-021-00670-x. Online ahead of print.PMID: 34608240

https://pubmed.ncbi.nlm.nih.gov/34608240/

Shinya Ito, Kazuhiro Nagata

Quality Control of Procollagen in Cells

Annu Rev Biochem. 90:631-658 (2021)

https://pubmed.ncbi.nlm.nih.gov/33823651/

Taira Y, Ikuta Y, Inamori S, Nunome M, Nakano M, Suzuki T, Matsuda Y, Tsudzuki M, Teramoto M, Iida H, Kondoh H.

The formation of multiple pituitary pouches from the oral ectoderm causes ectopic lens development in hedgehog signaling-defective avian embryos.

Dev Dyn. 2020 249(12):1425-1439. doi: 10.1002/dvdy.222.

Yuxia Zhanga, Michio Inoue, Akihisa Tsutsumi, Satoshi Watanabe, Tomohiro Nishizawac, Kazuhiro Nagata, Masahide Kikkawa and Kenji Inaba

Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail

Science Advance 6(33) eabb0147 (2020)
doi.org/10.1101/2020.03.28.012849.

https://advances.sciencemag.org/content/6/33/eabb0147

Iwanami N, Takeshita K, Lawir DF, Suetake I, Tajima S, Sikora K, Trancoso I, ÓMeara C, Siamishi I, Takahama Y, Furutani-Seiki M, Kondoh H, Yonezawa Y, Schorpp M, Boehm T.

Epigenetic Protection of Vertebrate Lymphoid Progenitor Cells by Dnmt1.

iScience. 2020 24;23(7):101260. doi: 10.1016/j.isci.2020.101260.

A. Kohler, M. Morgelin, J.M. Gebauer, S. Ocal, T. Imhof, M. Koch, K. Nagata, M. Paulsson, M. Aumailley, U. Baumann, F. Zacke & G. Sengle:

New specific Hsp47 functions in collagen subfamily chaperoning.

FASEB J. 34:12040-12052 (2020)

https://faseb.onlinelibrary.wiley.com/doi/10.1096/fj.202000570R

Yo-hei Yamamoto, Ayano Kasai, Hiroko Omori, Tomoe Takino, Munechika Sugihara, Tetsuo Umemoto, Maho Hamasaki, Tomohisa Hatta, Tohru Natsume, Richard I. Morimoto, Ritsuko Arai, Satoshi Waguri, Miyuki Sato, Ken Sato, Shoshana Bar-Nun,Tamotsu Yoshimori, Takeshi Noda and Kazuhiro Nagata

ERdj8 governs the size of autophagosomes during the formation process

J. Cell. Biol. 219(8): e201903127 (2020)

https://rupress.org/jcb/article/219/8/e201903127/151832/

Inamori S, Fujii M, Satake S, Iida H, Teramoto M, Sumi T, Meno C, Ishii Y, Kondoh H.

Modeling early stages of endoderm development in epiblast stem cell aggregates with supply of extracellular matrices.

Dev Growth Differ. 2020 62(4):243-259. doi: 10.1111/dgd.12663.

Iida H, Furukawa Y, Teramoto M, Suzuki H, Takemoto T, Uchikawa M, Kondoh H.

Sox2 gene regulation via the D1 enhancer in embryonic neural tube and neural crest by the combined action of SOX2 and ZIC2.

Genes Cells. 2020 25(4):242-256. doi: 10.1111/gtc.12753.

M. Yoshida, M. Saito, S. Ito, K. Ogawa, N. Goshima, K. Nagata & T. Doi

Structure-Activity Relationship Study on Col-003, a Protein-Protein Interaction Inhibitor between Collagen and Hsp47.

Chem Pharm Bull. 68(3)：220-226 (2020)

https://www.jstage.jst.go.jp/article/cpb/68/3/68_c19-00634/_article

Teramoto M, Sugawara R, Minegishi K, Uchikawa M, Takemoto T, Kuroiwa A, Ishii Y, Kondoh H.

The absence of SOX2 in the anterior foregut alters the esophagus into trachea and bronchi in both epithelial and mesenchymal components.

Biol Open. 2020 9(2):bio048728. doi: 10.1242/bio.048728.

G. Xiong, J. Chen, G. Zhang, S. Wang, K. Kawasaki, J. Zhu, Y. Zhang, K. Nagata, Z. Li, BP. Zhou, R. Xu

Hsp47 promotes cancer metastasis by enhancing collagen-dependent cancer cell-platelet interaction.

Proc Natl Acad Sci U S A. 117 (7) :3748-3758 (2020)
doi.org/10.1073/pnas.1911951117

https://www.pnas.org/content/117/7/3748

S. Ito, M. Saito, M. Yoshida, K. Takeuchi, T. Doi & K. Nagata

A BRET-based assay reveals collagen-Hsp47 interaction dynamics in the endoplasmic reticulum and small-molecule inhibition of this interaction.

J Biol Chem. 294(44):15962-15972 (2019)
doi: 10.1074/jbc.RA119.010567

https://www.jbc.org/article/S0021-9258(20)30456-7/

KK. Fujii, Y. Taga, T. Sakai, S. Ito, S. Hattori, K. Nagata & T. Koide

Lowering the culture temperature corrects collagen abnormalities caused by HSP47 gene knockout.

Sci Rep.9(1):17433. (2019)
DOI:10.1038/s41598-019-53962-0

https://www.nature.com/articles/s41598-019-53962-0

H. Khalil, O. Kanisicak, RJ. Vagnozzi, AK. Johansen, BD. Maliken, V. Prasad, JG. Boyer, MJ. Brody, T. Schips, KK. Kilian, RN. Correll, K. Kawasaki, K. Nagata & JD. Molkentin

Cell-specific ablation of Hsp47 defines the collagen-producing cells in the injured heart.

JCI Insight 4(15):e128722 (2019)

https://insight.jci.org/articles/view/128722

M. Inoue, N. Sakuta, S. Watanabe, Y. Zhang, K. Yoshikaie, R. Ushioda, Y. Kato, J. Takeda, T. Tsukazaki, K. Nagata & K. Inaba

Structural Basis of Sarco/Endoplasmic Reticulum Ca2+-ATPase 2b Regulation via Transmembrane Helix Interplay

Cell Rep.27(4)1221-1230 (2019)
10.1016/j.celrep.2019.03.106

https://www.sciencedirect.com/science/article/pii/S221112471930453X

S. Ito & K. Nagata

Roles of the endoplasmic reticulum-resident, collagen-specific molecular chaperone Hsp47 in vertebrate cells and human disease.

J Biol Chem. 294(6):2133-2141 (2019)
DOI: 10.1074/jbc.TM118.002812

https://www.jbc.org/article/S0021-9258(20)36857-5/

M. Sugihara, D. Morito, S. Ainuki, Y. Hirano, K. Ogino, A. Kitamura, H. Hirata & K. Nagata

The AAA+ ATPase/ubiquitin ligase mysterin cytoplasmic lipid droplets

J. Cell. Biol. 218(3):949-960 (2019)
DOI: 10.1083/jcb.201712120 | Published January 31, 2019

https://rupress.org/jcb/article/218/3/949/120793/

Motojima F, Fujii K, Yoshida M.

Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.

J Biochem. 2018 Nov 1;164(5):369-379. doi: 10.1093/jb/mvy061.PMID: 30053017 Free PMC article.

https://pubmed.ncbi.nlm.nih.gov/30053017/

R. Ushioda & K. Nagata

Redox-Mediated Reguiatory Mechanisms of Endplasmic Reticulum Homeostasis.

Cold Spring Harbor Perspectives in Biology”Protein Homeostasis SECOND EDITION”
Cold Spring Harbor Laboratory press 1;11(5), (2019)
doi: 10.1101/cshperspect.a033910

https://cshperspectives.cshlp.org/content/11/5/a033910

H.H. Kampinga, C. Andreasson, A. Barducci, M.E.Cheetham, D. Cyr, C. Emanuelsson, P. Genevaux, J.E. Gestwicki, P. Goloubinoff, J. Huerta-Cepas, J. Kirstein, K. Liberek, M.P. Mayer, K. Nagata, N.B. Nillegoda, P. Pulido, C. Ramos, P. De Los Rios, S. Rospert, R. Rosenzweig, C. Sahi, M. Taipale, B. Tomiczek, R. Ushioda, J.C. Young,R. Zimmermann, A. Zylicz, M. Zylicz, E.A. Craig & J. Marszalek

Function, evolution, and structure of J-domain proteins.

Cell Stress and Chaperones 24(1):7-15 (2019)
doi: 10.1007/s12192-018-0948-4. Epub 2018 Nov 26.

https://link.springer.com/article/10.1007%2Fs12192-018-0948-4

Saita E, Suzuki T, Kinosita K Jr, Yoshida M.

Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion.

Proc Natl Acad Sci USA. 2015 Aug 4;112(31):9626-31. doi: 10.1073/pnas.1422885112. Epub 2015 Jul 20.PMID: 26195785 Free PMC article.

https://pubmed.ncbi.nlm.nih.gov/26195785/

Suzuki T, Tanaka K, Wakabayashi C, Saita E, Yoshida M.

Chemomechanical coupling of human mitochondrial F1-ATPase motor.

Nat Chem Biol. 2014 Nov;10(11):930-6. doi: 10.1038/nchembio.1635. Epub 2014 Sep 21.PMID: 25242551

https://pubmed.ncbi.nlm.nih.gov/25242551/