Publications | Kimata group English

Original Research papers

59. Fauzee YNBM, Yoshida Y, Kimata Y

"Endoplasmic stress sensor Ire1 is involved in cytosolic/nuclear protein quality control in Pichia pastoris cells independent of HAC1"

Front. Microbiol. Vol.14, 1157146 (2023)

58. Phuong HT, Ishiwata-Kimata Y, Kimata Y

"An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response"

Biochem. Biophys. Res. Commun. Vol. 667, 58-63 (2023)

https://pubmed.ncbi.nlm.nih.gov/37209563/

57. Nguyen PTM, Ishiwata-Kimata Y, Kimata Y

"Fast-growing Saccharomyces cerevisiae cells with a constitutive unfolded protein response and their potential for lipidic molecule production."
Appl. Environ. Microbiol. Vol.88, e0108322 (2022)

https://pubmed.ncbi.nlm.nih.gov/36255243/

56. Hata T, Ishiwata-Kimata Y, Kimata Y

"Self-association status-dependent inactivation of the endoplasmic reticulum stress sensor Ire1 by C-terminal tagging with artificial peptides"

Biosci. Biotechnol. Biochem. Vol. 86, 739-746 (2022)

https://pubmed.ncbi.nlm.nih.gov/35285870/

55. Hata T, Ishiwata-Kimata Y, Kimata Y

"Induction of the unfolded protein response at high temperature in Saccharomyces cerevisiae"

Int. J. Mol. Sci. Vol.23, 1669 (2022)

https://pubmed.ncbi.nlm.nih.gov/35163590/
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54. Ishiwata-Kimata Y, Le QG, Kimata Y

"Induction and aggravation of the endoplasmic-reticulum stress by membrane-lipid metabolic intermediate phosphatidyl-N-monomethylethanolamine"

Front. Cell Dev. Biol. Vol.9, 743018 (2022)

https://pubmed.ncbi.nlm.nih.gov/35071223/

53. Phuong TH, Ishiwata-Kimata Y, Nishi Y, Oguchi N, Takagi H, Kimata Y

"Aeration mitigates endoplasmic reticulum stress in Saccharomyces cerevisiae even without mitochondrial respiration."

Microb. Cell Vol.8, 77-86 (2021)

https://pubmed.ncbi.nlm.nih.gov/33816593/

52. Le QG, Ishiwata-Kimata Y, Phuong TH, Fukunaka S, Kohno K, Kimata Y

"The ADP-binding kinase region of Ire1 directly contributes to its responsiveness to endoplasmic reticulum stress."

Sci. Rep. Vol.11, 4506 (2021)

https://pubmed.ncbi.nlm.nih.gov/33627709/

51. Fauzee YNBM, Taniguchi N, Ishiwata-Kimata Y, Takagi H, Kimata Y

"The unfolded protein response in Pichia pastoris without external stressing stimuli."

FEMS Yeast Res. Vol.20 foaa053 (2020)

https://pubmed.ncbi.nlm.nih.gov/33775971/

50. Tran DM, Ishiwata-Kimata Y, Mai TC, Kubo M, Kimata Y.

“The unfolded protein response alongside the diauxic shift of yeast cells and its involvement in mitochondria enlargement.”

Sci. Rep. Vol. 9, 12780 (2019)

https://www.ncbi.nlm.nih.gov/pubmed/31484935

49. Mai TC, Ishiwata-Kimata Y, Le QG, Kido H, Kimata Y.

“Dispersion of Endoplasmic Reticulum-associated Compartments by 4-phenyl Butyric Acid in Yeast Cells.”

Cell. Struct. Funct. Vol. 44, 173-182 (2019)

https://www.ncbi.nlm.nih.gov/pubmed/31619600

48. Nguyen PTM, Ishiwata-Kimata Y, Kimata Y.

“Monitoring ADP/ATP ratio in yeast cells using the fluorescent-protein reporter PercevalHR.”

Biosci. Biotechnol. Biochem. Vol. 83, 824-828 (2019)

https://www.ncbi.nlm.nih.gov/pubmed/30704350

47. Tran DM, Takagi H, Kimata Y.

“Categorization of endoplasmic reticulum stress as accumulation of unfolded proteins or membrane lipid aberrancy using yeast Ire1 mutants.”

Biosci. Biotechnol. Biochem. Vol. 83, 326-329 (2019)

https://www.ncbi.nlm.nih.gov/pubmed/30319071

46. Mai TC, Munakata T, Tran DM, Takagi H, Kimata Y.

“A chimeric mutant analysis in yeast cells suggests BiP independent regulation of the mammalian endoplasmic reticulum-stress sensor IRE1α.”

Biosci. Biotechnol. Biochem. Vol. 82, 1527-1530 (2018)

https://www.ncbi.nlm.nih.gov/pubmed/29806786

45. Mai CT, Le QG, Ishiwata-Kimata Y, Takagi H, Kohno K, Kimata Y.

“4-Phenylbutyrate suppresses the unfolded protein response without restoring protein folding in Saccharomyces cerevisiae.”

FEMS Yeast Res. Vol. 18, foy016 (2018)

https://www.ncbi.nlm.nih.gov/pubmed/29452364

44. Itooka K, Takahashi K, Kimata Y, Izawa S.

“Cold atmospheric pressure plasma causes protein denaturation and endoplasmic reticulum stress in Saccharomyces cerevisiae.”

Appl. Microbiol. Biotechnol. Vol. 102, 2279-2288 (2018)

https://www.ncbi.nlm.nih.gov/pubmed/29356871

43. Kawazoe N, Kimata Y, Izawa S.

“Acetic acid causes endoplasmic reticulum stress and induces the unfolded protein response in Saccharomyces cerevisiae.”

Front. Microbiol. Vol. 8, 1192 (2017)

https://www.ncbi.nlm.nih.gov/pubmed/28702017

42. Le QG, Ishiwata-Kimata Y, Kohno K, Kimata Y.

“Cadmium impairs protein folding in the endoplasmic reticulum and induces the unfolded protein response.”

FEMS Yeast Res. Vol.16, fow049 (2016)

https://www.ncbi.nlm.nih.gov/pubmed/27298227

41. Mathuranyanon R, Tsukamoto T, Takeuchi A, Ishiwata-Kimata Y, Tsuchiya Y, Kohno K, Kimata Y.

“Tight regulation of the unfolded protein sensor Ire1 by its intramolecularly antagonizing subdomain.”

J. Cell Sci. Vol.128, 1762-172 (2015)

https://www.ncbi.nlm.nih.gov/pubmed/25770101

40. Mochizuki T, Kimata Y, Uemura S, Abe F.

“Retention of chimeric Tat2-Gap1 permease in the endoplasmic reticulum induces unfolded protein response in Saccharomyces cerevisiae.”

FEMS Yeast Res. Vol.15, fov044 (2015)

https://www.ncbi.nlm.nih.gov/pubmed/26071436

39. Miyagawa D, Ishiwata-Kimata Y, Kohno K, Kimata Y

“Ethanol stress impairs protein folding in the endoplasmic reticulum and activates Ire1 in Saccharomyces cerevisiae.”

Biosci. Biotechnol. Biochem. Vol.78,1389-1391 (2014)

https://www.ncbi.nlm.nih.gov/pubmed/25130742

38. Ishiwata-Kimata Y, Yamamoto YH, Takizawa K, Kohno K, Kimata Y

F-actin and a type-II myosin are required for efficient clustering of the ER stress sensor Ire1.

Cell Struct. Funct. Vol.38, 135-143 (2013)

https://www.ncbi.nlm.nih.gov/pubmed/23666407

37. Ishiwata-Kimata Y, Promlek T, Kohno K, Kimata Y

“BiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response.”

Genes Cells Vol.18, 288-301 (2013)

https://www.ncbi.nlm.nih.gov/pubmed/23387983

36. Nguyen TSL, Kohno K, Kimata Y

“Zinc depletion activates the endoplasmic reticulum-stress sensor Ire1 via pleiotropic mechanisms.”

Biosci. Biotechnol. Biochem. Vol. 77, 1337-1339 (2013)

https://www.ncbi.nlm.nih.gov/pubmed/23748779

35. Promlek T, Ishiwata-Kimata Y, Shido M, Sakuramoto M, Kohno K, Kimata Y

“Membrane aberrancy and unfolded aroteins activate the endoplasmic reticulum-stress sensor Ire1 by different manners.”

Mol. Biol. Cell Vol.22, 3520-3532 (2011)

https://www.ncbi.nlm.nih.gov/pubmed/21775630

34. Yanagitani K, Kimata Y, Kadokura H, Kohno K

“Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA.”

Science Vol.331, 586-589 (2011)

https://www.ncbi.nlm.nih.gov/pubmed/21233347

33. Yamamoto YH, Kimura T, Momohara S, Takeuchi M, Tani T, Kimata Y, Kadokura H, Kohno K

“A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR.”

Cell Struct. Funct. Vol.35, 107-116 (2010)

https://www.ncbi.nlm.nih.gov/pubmed/21150129

32. Yanagitani K, Imagawa Y, Iwawaki T, Hosoda A, Saito M, Kimata Y, Kohno K

“Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA.”

Mol. Cell Vol.34, 191-200 (2009)

https://www.ncbi.nlm.nih.gov/pubmed/19394296

31. Oikawa D, Kimata Y, Kohno K, Iwawaki T

“Activation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins.”

Exp. Cell Res. Vol. 315, 2496-2504 (2009)

https://www.ncbi.nlm.nih.gov/pubmed/19538957

30. Takeuchi M, Kimata Y, Kohno K

“Saccharomyces cerevisiae Rot1 Is an essential molecular chaperone in the endoplasmic reticulum.”

Mol. Biol. Cell Vol.19, 3514-3525 (2008)

https://www.ncbi.nlm.nih.gov/pubmed/18508919

29. Kimata Y, Ishiwata-Kimata Y, Ito T, Hirata A, Suzuki T, Oikawa D, Takeuchi M, Kohno K

“Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.”

J. Cell Biol. Vol.179, 75-86 (2007)

https://www.ncbi.nlm.nih.gov/pubmed/17923530

28. Kimura Y, Saito M, Kimata Y, Kohno K

“Transgenic mice expressing a fully nontoxic diphtheria toxin mutant, not CRM197 mutant, acquire immune tolerance against diphtheria toxin.”

J. Biochem. Vol.142, 105-112 (2007)

https://www.ncbi.nlm.nih.gov/pubmed/17522091

27. Oikawa D, Kimata Y, Kohno K

“Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1.”

J. Cell Sci. Vol.120, 1681-1688 (2007)

https://www.ncbi.nlm.nih.gov/pubmed/17452628

26. Takeuchi M, Kimata Y, Hirata A, Oka M, Kohno K

“Saccharomyces cerevisiae Rot1p Is an ER-Localized membrane protein that may function with BiP/Kar2p in protein folding.”

J. Biochem. Vol.139, 597-605 (2006)

https://www.ncbi.nlm.nih.gov/pubmed/16567426

25. Kimata Y, Ishiwata-Kimata Y, Yamada S, Kohno K

“Yeast unfolded protein response pathway regulates expression of genes for anti-oxidative stress and for cell surface proteins.”

Genes Cells. Vol.11, 59-69 (2006)

https://www.ncbi.nlm.nih.gov/pubmed/16371132

24. Oikawa D, Kimata Y, Takeuchi M, Kohno K

“An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1.”

Biochem J. Vol.391, 135-142 (2005)

https://www.ncbi.nlm.nih.gov/pubmed/15954865

23. Kimata Y, Oikawa D, Shimizu Y, Ishiwata-Kimata Y, Kohno, K

“A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1.”

J. Cell Biol. Vol.167, 445-456 (2004)

https://www.ncbi.nlm.nih.gov/pubmed/15520230

22. Kimata Y, Kimata YI, Shimizu Y, Abe H, Farcasanu IC, Takeuchi M, Rose MD, Kohno K

“Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.”

Mol. Biol. Cell Vol.14, 2559-2569 (2003)

https://www.ncbi.nlm.nih.gov/pubmed/12808051

21. Ohdate H, Lim CR, Kokubo T, Matsubara K, Kimata Y, Kohno K

“Impairment of the DNA binding activity of the TATA-binding protein renders the transcriptional function of Rvb2p/Tih2p, the yeast RuvB-like protein, essential for cell growth.”

J. Biol. Chem. Vol.278, 14647-14656 (2003)

https://www.ncbi.nlm.nih.gov/pubmed/12576485

20. Hosoda A, Kimata Y, Tsuru A, Kohno K

“JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs.”

J. Biol. Chem. Vol.278, 2669-2676 (2003)

https://www.ncbi.nlm.nih.gov/pubmed/12446677

19. Fujioka Y, Kimata Y, Nomaguchi K, Watanabe K, Kohno K

“Identification of a novel non-structural maintenance of chromosomes (SMC) component of the SMC5/SMC6 complex involved in DNA repair.”

J. Biol. Chem. Vol.277, 21585-21591 (2002)

https://www.ncbi.nlm.nih.gov/pubmed/11927594

18. Okushima Y, Koizumi N, Yamaguchi Y, Kimata Y, Kohno K, Sano H

“Isolation and Characterization of a Putative Transducer of Endoplasmic Reticulum Stress in Oryza sativa.”

Plant Cell Physiol. Vol.43, 532-539 (2002)

https://www.ncbi.nlm.nih.gov/pubmed/12040100

17. Koizumi N, Martinez I, Kimata Y, Kohno K, Sano H, Chrispeels MJ

“Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum located transmembrane protein kinases.”

Plant Physiol. Vol.127, 949-962 (2001)

https://www.ncbi.nlm.nih.gov/pubmed/11706177

16. Saito M, Iwawaki T, Taya C, Yonekawa H, Noda M, Inui Y, Mekada E, Kimata Y, Tsuru A, Kohno K

“Diphtheria toxin receptor-mediated conditional and targeted cell ablation in transgenic mice.”

Nature Biotechnol. Vol.19, 746-750 (2001)

https://www.ncbi.nlm.nih.gov/pubmed/11479567

15. Iwawaki T, Hosoda A, Okuda T, Kamigori Y, Nomura-Furuwatari C, Kimata Y, Tsuru A, Kohno K

“Translation control by ER transmembrane kinase/ribonuclease IRE1 under ER stress.”

Nature Cell Biol. Vol.3, 158-164 (2001)

https://www.ncbi.nlm.nih.gov/pubmed/11175748

14. Kimata Y, Ooboki K, Nomura-Furuwatari C, Hosoda A, Tsuru A, Kohno K

“Identification of a novel mammalian endoplasmic reticulum-resident KDEL protein using an EST database motif search.”

Gene Vol.261, 321-327 (2000)

https://www.ncbi.nlm.nih.gov/pubmed/11167020

13. Yoshizawa F, Miura Y, Tsurumaru K, Kimata Y, Yagasaki K, Funabiki R

“Elongation factor 2 in the liver and skeletal muscle of mice is decreased by starvation.”

Biosci. Biotechnol. Biochem. Vol.64, 2482-2485 (2000)

https://www.ncbi.nlm.nih.gov/pubmed/11193422

12. Okamura K, Kimata Y, Higashio H, Tsuru A, Kohno K

“Dissociation of Kar2p/BiP from an endoplasmic reticulum sensory molecule, Ire1p, triggers unfolded protein response in yeast.”

Biochem. Biophys. Res. Commun. Vol.279, 445-450 (2000)

https://www.ncbi.nlm.nih.gov/pubmed/11118306

11. Lim CR, Kimata Y, Ohdate H, Kokubo T, Kikuchi N, Horigome T, Kohno K

“The Saccharomyces cerevisiae RuvB-like protein, Tih2p is required for cell cycle progression.”

J. Biol. Chem. Vol.275, 22409-22417 (2000)

https://www.ncbi.nlm.nih.gov/pubmed/10787406

10. Higashio H, Kimata Y, Kiriyama T, Hirata A, Kohno K

“Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum.”

J. Biol. Chem. Vol.275, 17900-17908 (2000)

https://www.ncbi.nlm.nih.gov/pubmed/10749860

9. Kimata Y, Higashio H, Kohno K

“Impaired proteasome function rescues thermosensitivity of yeast cells lacking the coatomer subunit epsilon-COP.”

J. Biol. Chem. Vol.275, 10655-10660 (2000)

https://www.ncbi.nlm.nih.gov/pubmed/10744762

8. Kimata Y, Lim CR, Kiriyama T, Nara A, Hirata A, Kohno K

“Mutation of the yeast epsilon-COP gene ANU2 causes abnormal nuclear morphology and defects in intracellular vesicular transport.”

Cell Struct. Funct. Vol.24, 197-208 (1999)

https://www.ncbi.nlm.nih.gov/pubmed/10532354

7. Oka M, Nakai M, Endo T, Lim CR, Kimata Y, Kohno K

“Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae.”

J. Biol. Chem. Vol.273, 29727-29737 (1998)

https://www.ncbi.nlm.nih.gov/pubmed/9792686

6. Kimata Y, Iwaki M, Lim CR, Kohno K

“A novel mutation which enhances the fluorescence of green fluorescent protein at high temperatures.”

Biochem. Biophys. Res. Commun. Vol.232, 69-73 (1997)

https://www.ncbi.nlm.nih.gov/pubmed/9125154

5. Oka M, Kimata Y, Mori K, Kohno K

“Saccharomyces cerevisiae KAR2 (BiP) gene expression is induced by loss of cytosolic HSP70/Ssa1p through a heat shock element-mediated pathway.”

J. Biochem. Vol.121, 578-584 (1997)

https://www.ncbi.nlm.nih.gov/pubmed/9133628

4. Lim CR, Kimata Y, Oka M, Nomaguchi K, Kohno K

“Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1.”

J. Biochem. Vol.118, 13-17 (1995)

https://www.ncbi.nlm.nih.gov/pubmed/8537302

3. Kimata Y, Kohno K

“Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth.”

J. Biol. Chem. Vol.269, 13497-134501 (1994)

https://www.ncbi.nlm.nih.gov/pubmed/8175783

2. Kimata Y, Harashima S, Kohno K

“Expression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation factor 2 in Saccharomyces cerevisiae.”

Biochem. Biophys. Res. Commun. Vol.191, 1145-1151 (1993)

https://www.ncbi.nlm.nih.gov/pubmed/8466491

1. Masui M, Tsuchida K, Kimata Y, Ozaki S

“Epoxidation catalyzed by manganese(III) tetraphenylporphyrin chloride using dioxygen activated by a novel system containing N-hydroxyphthalimide and styrene.”

Chem. Pharm. Bull. Vol.35, 3078-3081 (1987)

Reviews and Book Chapters

8. Le QG, Kimata Y.

"Multiple ways for stress sensing and regulation of the endoplasmic reticulum-stress sensors."

Cell Struct. Funct. Vol. 46, 37-49 (2021)