原著論文（稲田）

  • Matsuo, Y.* and Inada, T.*
    Ribosome collision sensor Hel2 functions as preventive quality control in the secretory pathway.
    Cell Rep. (2021) doi: 10.1016/j.celrep.2021.108877 (2021) (Press release)
  • Mizuno, M.#, Ebine, S.#, Shounai, O., Nakajima, S., Tomomatsu, S., Ikeuchi, K., Matsuo, Y., and
    Inada, T.* (#Equal contribution)
    The nascent polypeptide in the 60S subunit determines the Rqc2-dependency of ribosomal
    quality control.
    Nucleic Acid Research doi: 10.1093/nar/gkab005 (2021) (Press release)
  • Udagawa, T.#*, Seki, M.#, Okuyama, T.#, Adachi, S., Natsume, T., Noguchi, T., Matsuzawa, A.,
    Inada, T.* (#Equal contribution)
    Failure to degrade CAT-tailed proteins disrupts neuronal morphogenesis and cell survival.
    Cell Rep. doi: 10.1016/j.celrep.2020.108599 (2021) (Press release)
  • Watada, E., Li S., Hori, Y., Fujiki, K., Shirahige, K., Inada, T., Kobayashi, T.*
    Age-Dependent Ribosomal DNA Variations in Mice
    Mol. Cell. Biol. doi: 10.1128/MCB.00368-20 (2020)
  • Matsuki, Y.#, Matsuo, Y.#, Nakano, Y., Iwasaki, S., Yoko, H., Udagawa, T., Li, S., Saeki, Y., Yoshihisa, T., Tanaka, K., Ingolia, NT., and Inada, T.* (#Equal contribution)
    Ribosomal protein S7 ubiquitination during ER stress in yeast is associated with selective mRNA translation and stress outcome
    Sci. Rep. doi:10.1038/s41598-020-76239-3 (2020)
  • Nobuta, R., Machida, K., Sato, M., Hashimoto, S., Toriumi, Y., Nakajima, S., Suto, D., Imataka, H.* and Inada, T.*
    eIF4G-driven translation initiation of downstream ORFs in mammalian cells
    Nucleic Acid Research doi: 10.1093/nar/gkaa728 (2020)
  • Matsuki, Y., Saito, T., Nakano, Y., Hashimoto, S., Matsuo, Y., Inada, T.*
    Crucial role of leaky initiation of uORF3 in the downregulation of HNT1 by ER stress
    Biochem Biophys Res Commun. doi: 10.1016/j.bbrc.2020.04.104 (2020)
  • Han, P., Shichino, Y., Schneider-Poetsch, T., Mito, M., Hashimoto, S., Udagawa, T., Kohno, K., Yoshida, M., Mishima, Y., Inada, T., Iwasaki, S.*
    Genome-wide Survey of Ribosome Collision
    Cell Reports doi: https://doi.org/10.1016/j.celrep.2020.107610 (2020)
  • Nakagawa, T., Hattori S., Nobuta R., Kimura R., Nakagawa M., Matsumoto M., Nagasawa Y., Funayama R., Miyakawa T., Inada T., Osumi N., Nakayama KI., Nakayama K.*
    The Autism-Related Protein SETD5 Controls Neural Cell Proliferation through Epigenetic Regulation of rDNA Expression
    iScience doi:10.1016/j.isci.2020.101030 (2020)
  • Buschauer, R.#, Matsuo, Y.#, Sugiyama, T., Chen, Y., Alhusaini, N., Sweet, T., Ikeuchi, K., Cheng, J., Matsuki, Y., Nobuta, R., Gilmozzi, A., Berninghausen, O., Tesina, P., Becker, T., Coller, J.*, Inada, T.*, Beckmann, R.* (#Equal contribution)
    The Ccr4-Not complex monitors the translating ribosome for codon optimality
    Science doi: 10.1126/science.aay6912 (2020)
  • Matsuo, Y.#, Tesina, P.#, Nakajima, S., Mizuno, M., Endo, A., Buschauer, R., Cheng, J., Shounai, O., Ikeuchi, K., Saeki, Y., Becker, T., *Beckmann, R. and Inada, T.* (#Equal contribution)
    RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1
    Nat. Struc. Mol. Biol. doi: 10.1038/s41594-020-0393-9 (2020)
  • Inada, T.*
    Quality controls induced by aberrant translation.
    Nucl. Acids Res. doi:10.1093/nar/gkz1201. (2020)
  • Hashimoto, S.#, Sugiyama, T.#, Yamazaki, R., Nobuta, R. and Inada, T.* (#Equal contribution)
    Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells
    Sci. Rep. 10: 3422 /doi.org/10.1038/s41598-020-60241-w (2020)
  • Yasuda, S.#, Tsuchiya, H.#, Kaiho, A.#, Guo, Q., Ikeuchi, K., Endo, A., Arai, N., Ohtake, F., Murata, S., Inada, T., Baumeister, Wolfgang.,
    Fernández-Busnadiego, R., Tanaka, K.* and Saeki, Y.* (#Equal contribution)
    Stress- and ubiquitylation-dependent phase separation of the proteasome
    Nature doi: 10.1038/s41586-020-1982-9. (2020)
  • Inada, T.*
    The proteasome’s balancing act.
    Nat. Plants doi: 10.1038/s41477-019-0551-4 (2019)
  • Inada, T.*
    tRNA recycling on stalled ribosomes.
    Nat. Struct. Mol. Biol. ;26(5):340-342. (2019)
  • Ikeuchi, K., Izawa, T., Inada, T.*
    Recent Progress on the Molecular Mechanism of Quality Controls Induced by Ribosome Stalling.
    Front Genet. ;9, 743-. (2019)
  • Su, T.#, Izawa, T.#, Thoms, M., Yamashita, Y., Cheng, J., Berninghausen, O., Hartl,U., Inada, T., Neupert, W.* and Beckmann, R.* (#Equal contribution)
    Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis
    Nature doi: 10.1038/s41586-019-1307-z. (2019)
  • Hashimoto, S., Nobuta, R., Izawa, T. and Inada, T.*
    Translation arrest as a protein quality control system for aberrant translation of the 3′-UTR in mammalian cells
    FEBS Letters (2019) DOI:10.1002/1873-3468.13362
  • Sugiyama, T.1, Li, S.1, Kato, M.1, Ikeuchi, K., Ichimura, A., Matsuo, Y. and Inada, T.* (1Equal contribution)
    Sequential ubiquitination of ribosomal protein uS3 triggers the degradation of non-functional 18S rRNA
    Cell Reports (2019) DOI: https://doi.org/10.1016/j.celrep.2019.02.067.
  • Ikeuchi, K., Tesina, P., Matsuo, Y., Sugiyama, T., Cheng, J., Saeki, Y., Tanaka, K., Becker, T., Beckmann, R.*, Inada, T.*
    Collided ribosomes form a unique structural interface to induce Hel2‐driven quality control pathways
    EMBO J. 38 (2019). doi: 10.15252/embj.2018100276.
  • Inada, T.*
    The ribosome as a platform for mRNA and nascent polypeptide quality control.
    Trends Biochem. Sci. 42, 5-15 (2017)
  • Matsuo, Y., Ikeuchi, K., Saeki, Y., Iwasaki, S., Schmidt, C., Udagawa, T., Sato, F., Tsuchiya, H., Becker, T., Tanaka, K., Ingolia, NT., Beckmann, R. and Inada, T.*
    Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control.
    Nat. Commun. DOI 10.1038/s41467-017-00188-1 (2017)
  • Sugiyama T, Nobuta R, Ando K, Matsuki Y, Inada, T.*
    Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product. Biochem Biophys Res Commun. 488, 122-128. doi: 10.1016/j.bbrc.2017.05.0 (2017)
  • Ikeuchi, K., Yazaki, E., Kudo, K. and Inada, T.*
    Conserved functions of human Pelota in mRNA quality controls for nonstop mRNA.
    FEBS Let. 18, 3254-3263 (2016)
  • Miki, A., Galipon, J., Sawai, S., Inada, T., Ohta, K.*
    RNA decay systems enhance reciprocal switching of sense and antisense transcripts in response to glucose starvation.
    Genes Cells,21(12):1276-1289. (2016)
  • Ikeuchi, K. and Inada, T.*

    Ribosome-associated Asc1/RACK1 is required for endonucleolytic cleavage induced by stalled ribosome at the 3′ end of nonstop mRNA.
    Sci. Rep.6, 28234. (2016)

  • Tsuboi, T.#, Yamazaki, R.#, Nobuta, R., Ikecuhi, K., Makino, S., Ohtaki, Y., Suzuki, Y., Yoshihisa, T., Trotta, C. and Inada, T.* (#Equal contribution) 
    The tRNA Splicing Endonuclease Complex Cleaves the Mitochondria-localized CBP1 mRNA.
    J Biol. Chem. 290, 16021-16030. (2015)

  • Makino, S., Mishima, Y., Inoue, K. and Inada, T.*
    Roles of mRNA-fate modulators Dhh1 and Pat1 in TNRC6-dependent gene silencing recapitulated in yeast.
    J Biol. Chem. 290, 8331- 8347. (2015)

  • Tanaka, Y., Tsuda, S., Kunikata, H., Sato, J., Kokubun, T., Yasuda, M., Nishiguchi, KM., Inada, T., Nakazawa T.*
    Profiles of extracellular miRNAs in the aqueous humor of glaucoma patients assessed with a microarray system.
    Sci Rep. 4, 5089 (2014)

  • Inada, T.*, Makino, S.
    Novel roles of the multi-functional CCR4-NOT complex in post-transcriptional regulation.
    Front Genet. ;5, 135-. (2014)

  • Matsuda, R., Ikecuhi, K., Nomura, S. and Inada, T.*
    Protein quality control systems associated with No-Go and Nonstop mRNA surveillance in yeast.
    Genes Cells 19, 1-12. (2014)

  • Kuroha, K., Ando, K., Nakagawa, R., Inada, T.*
    The Upf complex interacts with aberrant products derived from mRNAs containing a premature termination codon and facilitates their proteasomal degradation.
    J Biol. Chem. 288, 28630-28640 (2013)

  • Galipon, J., Miki, A., Oda, A., Inada, T., Ohta, K.*
    Stress-induced lncRNAs evade nuclear degradation and enter the translational machinery.
    Genes Cells 18, 353-368 (2013).

  • Inada, T.*
    Ribosome as a hub for protein and mRNA quality control and gene regulation.
    Seikagaku. ;85, 932-937 (2013)
  • Inada, T.*
    Quality control systems for aberrant mRNAs induced by aberrant translation elongation and termination.
    Biochim Biophys Acta. ;1829, 634-642. (2013)

  • Iwasaki, YW.#, Kiga, K.#, Kayo, H., Fukuda-Yuzawa, Y., Weise, J., Inada, T., Tomita, M., Ishihama, Y., Fukao, T.* (#Equal contribution) 
    Global microRNA elevation by inducible Exportin 5 regulates cell cycle entry.
    RNA 19, 490-497. (2013)

  • Brandman, O., Ornstein, JS., Wong, D., Larson, A., Williams, C.C., Li, G.W., Zhou, S., King, D., Shen, P.S., Weibezahn, J., Dunn, J.G., Rouskin, S., Inada, T., Frost, A.*, Weissman, JS.*
    A ribosome-bound quality control complex triggers nascent peptides and signals translation stress
    Cell 151,1042-1054. (2012).

  • Tsuboi, T., Kuroha, K., Kudo, K., Makino, S., Inoue, E., Kashima, I. and Inada, T.*
    Dom34:Hbs1 Plays a General Role in Quality Control Systems by Dissociation of Stalled Ribosome at 3′ End of Aberrant mRNA.
    Mol. Cell 26, 518-529. (2012)

  • Izawa, T., Tsuboi, T., Kuroha, K., Inada, T., Nishikawa, SI.*, Endo T.*
    Roles of Dom34:Hbs1 in Nonstop Protein Clearance from Translocators for Normal Organelle Protein Influx.
    Cell Reports 2, 447-453. (2012)

  • Kuroha, K., Akamatsu, M., Dimitrova, L., Ito, T., Kato, Y., Shirahige K. and Inada, T.*
    RACK1 stimulates nascent polypeptide-dependent translation arrest.
    EMBO Reports 11, 956-961. (2010)

  • Mori, T., Ogasawara, C., Inada T., Englert, M., Beier, H., Takezawa, M., Endo, T., Yoshihisa, T.*
    Dual functions of yeast tRNA ligase in the unfolded protein response: unconventional cytoplasmic splicing of HAC1 pre-mRNA is not sufficient to release translational attenuation.
    Mol. Biol. Cell 21, 3722-3734. (2010)

  • Kuroha, K., Akamatsu, M., Dimitrova, L., Ito, T., Kato, Y. Shirahige, K. and Inada, T.*
    RACK1 stimulates nascent polypeptide-dependent translation arrest.
    EMBO Reports 11, 956-961. (2010)

  • Kobayashi, K. Kikuno, I. Kuroha, K. Saito, K. Ito, K. Ishitani, R*. Inada, T. and Nureki, O.*
    Structural Basis for mRNA Surveillance by Archaeal Pelota and GTP-bound EF1α Complex.
    Proc. Natl. Acad. Sci. USA 107, 17575-17579. (2010)

  • Tsuboi, T. and Inada, T.*
    Tethering of poly(A) binding protein interferes with non-translated mRNA decay from 5′ end in yeast.
    J. Biol. Chem. 285, 33589-33601. (2010)

  • Kuroha, K., Tatematsu, T. and Inada, T.*
    Upf1p stimulates proteasome-mediated degradation of the product derived from the specific nonsense-containing mRNA.
    EMBO Reports 10, 1265-1271. (2009)

  • Kuroha, K., Dimitrova, L., Tatematsu, T. and Inada, T.*
    Nascent peptide-dependent translation arrest leads to not4p-mediated protein degradation by the proteasome.
    J. Biol. Chem. 284, 10343-10352. (2009)

  • Endo, A., Matsumoto, M., Inada, T., Yamamoto, A., Nakayama, K.I., Kitamura, N. and Komada, M.*
    Nucleolar structure and function regulated by a deubiquitinating enzyme USP36.
    J. Cell Sci. 122, 678-685. (2009)

  • Kuroha , K., Horiguchi, N., Aiba, H. and Inada, T.*
    Analysis of nonstop mRNA translation in the absence of tmRNA in E.coli.
    Genes to Cells 14, 739-749. (2009)

  • Nukazuka, A., Fujisawa, H., Inada, T., Oda, Y., Takagi, S.*
    Semaphorin controls epidermal morphogenesis by stimulating mRNA translation via eIF2a in Caenorhabditis elegans.
    Genes Dev. 22, 1025-1036. (2008)

  • Ito-Harashima, S., Kuroha, K., Tatematsu, T. and Inada, T.*
    Translation of poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast.
    Genes Dev. 21, 519-524. (2007)

  • Inada, T.* and Aiba, H.
    Translation of aberrant mRNAs lacking a termination codon or with a shortened 3′-UTR is repressed after initiation in yeast.
    EMBO J. 24, 1584-1595. (2005)

  • Kawamoto, H., Morita, T., Shimizu, A., Inada, T., Aiba, H.*
    Implication of membrane localization of target mRNA in the action of a small RNA: mechanism of post-transcriptional regulation of glucose transporter in Escherichia coli. 
    Genes Dev. 19, 328-338. (2005)

  • Tadauchi, T.#, Inada, T.#, Matsumoto, K.* and Irie, K. (#Equal contribution)
    Post-transcriptional regulation of HO expression by the Mkt1-Pbp1 complex.
    Mol. Cell Biol. 24, 3670-3681. (2004)

  • Sunohara, T., Jojima, K., Tagami, H., Inada, T. and Aiba, H.*
    Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli.
    J. Biol. Chem. 279, 15368-15375. (2004)

  • Sunohara, T., Jojima, K., Yamamoto, Y., Inada, T. and Aiba, H.*
    Nascent peptide-mediated ribosome stalling at stop codons induces mRNA cleavages resulting in nonstop mRNAs that are recognized by tmRNA.
    RNA 10, 378-386. (2004)

  • El-Kazzaz, W.#, Morita, T.#, Tagami, H., Inada, T. and Aiba, H.* (#Equal contribution)
    Metabolic block at early stages of glycolytic pathway leads to the activation RcsC/B system via perturbation in dTDP-glucose synthesis in Escherichia coli.
    Mol. Microbiol. 51, 1117 –1128. (2004)

  • Morita, T., El-Kazzaz, W., Tanaka, Y., Inada, T. and Aiba, H.*
    Accumulation of glucose 6-phosphate or fructose 6-phosphate is responsible for destabilization of glucose transporter mRNA in Escherichia coli.
    J. Biol. Chem. 278, 15608-15614. (2003)

  • Yamamoto, Y., Sunohara, T., Jojima, K., Inada, T. and Aiba, H.*
    SsrA-mediated trans-translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs.
    RNA 9, 408-418. (2003)

  • Baron-Benhamou, J., Fortes, P., Inada, T., Preiss, T.*, Hentze, MW.
    The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast.
    RNA 9, 654-662. (2003)

  • Sunohara, T., Abo, T., Inada, T. and Aiba, H.*
    The C-terminal amino acid sequence of nascent peptide is a major determinant of SsrA tagging at all three stop codons.
    RNA 8, 1416-1427. (2002)

  • Inada, T., Winstall, E., Tarun, S. Z., Jr., Yates, J. R., 3rd, Schieltz, D. and Sachs, A. B.*
    One-step affinity purification of the yeast ribosome and its associated proteins and mRNAs.
    RNA 8, 948-958 (2002)

  • Kimata, K., Tanaka, Y., Inada, T. and Aiba, H.*
    Expression of the glucose transporter gene, ptsG, is regulated at the mRNA degradation step in response to glycolytic flux in Escherichia coli.
    EMBO J. 20, 3587-3595. (2001)

  • Fortes, P., Inada, T., Preiss, T., Hentze, M. W., Mattaj, I. W. and Sachs, A. B.*
    The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation.
    Mol. Cell 6, 191-196. (2000)

  • Inada, T., Abo, T., Ogawa, K. and Aiba, H.*
    SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon.
    EMBO J. 19, 3762-3769. (2000)

  • Tanaka, Y., Kimata, K., Inada, T., Tagami, H. and Aiba, H.*
    Negative regulation of the pts operon by Mlc: mechanism underlying glucose induction in Escherichia coli.
    Genes Cells 4, 391-399. (1999)

  • Dasgupta, S., Fernandez, L., Kameyama, L., Inada, T., Nakamura, Y., Pappas, A. and Court, D. L.*
    Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the Escherichia coli endoribonuclease RNase III–the effect of dsRNA binding on gene expression.
    Mol. Microbiol. 28, 629-640. (1998)

  • Hogema, B. M., Arents, J. C., Bader, R., Eijkemans, K., Inada, T., Aiba, H. and Postma, P. W.*
    Inducer exclusion by glucose 6-phosphate in Escherichia coli.
    Mol. Microbiol. 28, 755-765. (1998)

  • Kimata, K., Inada, T., Tagami, H. and Aiba, H.*
    A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli.
    Mol. Microbiol. 29, 1509-1519. (1998)

  • Takahashi, H., Inada, T., Postma, P. and Aiba, H.*
    CRP down-regulates adenylate cyclase activity by reducing the level of phosphorylated IIA(Glc), the glucose-specific phosphotransferase protein, in Escherichia coli.
    Mol. Gen. Genet. 259, 317-326. (1998)

  • Hogema, B. M., Arents, J. C., Inada, T., Aiba, H., van Dam, K. and Postma, P. W.*
    Catabolite repression by glucose 6-phosphate, gluconate and lactose in Escherichia coli.
    Mol. Microbiol. 24, 857-867. (1997)

  • Kimata, K., Takahashi, H., Inada, T., Postma, P. and Aiba, H.*
    cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli.
    Proc. Natl. Acad. Sci. USA 94, 12914-12919. (1997)

  • Inada, T., Kimata, K. and Aiba, H.*
    Mechanism responsible for glucose-lactose diauxie in Escherichia coli: challenge to the cAMP model.
    Genes Cells 1, 293-301. (1996)

  • Inada, T., Takahashi, H., Mizuno, T. and Aiba, H.*
    Down regulation of cAMP production by cAMP receptor protein in Escherichia coli: an assessment of the contributions of transcriptional and posttranscriptional control of adenylate cyclase.
    Mol. Gen. Genet. 253, 198-204. (1996)

  • Inada, T. and Nakamura, Y.*
    Autogenous control of the suhB gene expression of Escherichia coli.
    Biochimie 78, 209-212. (1996)

  • Tagami, H., Inada, T., Kunimura, T. and Aiba, H.*
    Glucose lowers CRP* levels resulting in repression of the lac operon in cells lacking cAMP.
    Mol. Microbiol. 17, 251-258. (1995)

  • Inada, T. and Nakamura, Y.*
    Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli.
    Biochimie 77, 294-302. (1995)

  • Powell, B. S., Court, D. L.*, Inada, T., Nakamura, Y., Michotey, V., Cui, X., Reizer, A., Saier, M. H., Jr. and Reizer, J.
    Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant.
    J. Biol. Chem. 270, 4822-4839. (1995)

  • Ishizuka, H., Hanamura, A., Inada, T. and Aiba, H.*
    Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: role of autoregulation of the crp gene.
    EMBO J. 13, 3077-3082. (1994)

  • Akiyama, Y., Inada, T., Nakamura, Y. and Ito, K.*
    SecY, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site.
    J. Bacteriol. 172, 2888-2893. (1990)

  • Inada, T., Court, D. L., Ito, K. and Nakamura, Y.*
    Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli.
    J. Bacteriol. 171, 585-587. (1989)

  • Inada, T., Kawakami, K., Chen, S. M., Takiff, H. E., Court, D. L. and Nakamura, Y.*
    Temperature-sensitive lethal mutant of era, a G protein in Escherichia coli.
    J. Bacteriol. 171, 5017-5024. (1989)

  • Kawakami, K., Inada, T., and Nakamura, Y.*
    Conditionally lethal and recessive UGA-suppressor mutations in the prfB gene encoding peptide chain release factor 2 of Escherichia coli.
    J. Bacteriol. 170, 5378-5381. (1988)