Kyushu University Academic Staff Educational and Research Activities Database
List of Papers
Takeshi Sekiguchi Last modified date:2022.01.04

Assistant Professor / Molecular Biology / Department of Molecular Biology / Faculty of Medical Sciences

1. Takeshi Sekiguchi, Takashi Ishii, Hideki Kobayashi, Nobuaki Furuno, WDR35 is involved in subcellular localization of acetylated tubulin in293T cells, Biochemical and Biophysical Research Communications,, 547, 169-175, 2021.04, WDR35/IFT121 is an intraflagellar transport protein in primary cilia, which is associated with RagA, an
mTORC1-activating protein. To elucidate the functions of the interaction between WDR35 and RagA in
primary cilia, as well as mTOR signaling, we identified WDR35-interacting proteins using mass spectrometry.We found that WDR35 associates with CCT complex proteins including TCP1/CCT1, which act asmolecular chaperones for a-tubulin folding. Immunostaining showed that acetylated a-tubulin was
concentrated in the vicinity of primary cilia in 293T cells. In contrast, acetylated tubulin was dispersed inWDR35 partial knockout cells established from 293T cells. Similarly, scattered subcellular localization ofacetylated tubulin was observed in RagA knockout cells. RagA was present in the primary cilia of NIH3T3cells, and the GDP form of RagA exhibited strong binding to WDR35 and negative regulation of primarycilium formation. These results suggest that WDR35 is involved in the subcellular localization of acetylatedtubulin in primary cilia via its interactions with TCP1 and/or RagA family proteins..
2. Pazil Abdul-Patah, Hiroshi Sasaki, Takeshi Sekiguchi, Md Nor Shukor, Nur Syafika Mohd-Yusof, Muhammad Abu Bakar Abdul-Latiff & Badrul Munir Md-Zain, Molecular DNA-based spatial mapping technique predicting diversity and distribution of otters (Lutrinae) in Peninsular Malaysia using non-invasive fecal samples., Mammal Research,, 2020.08.
3. Takeshi Sekiguchi, Nobuaki Furuno, Takashi Ishii, Eiji Hirose, Fumiko Sekiguchi, Yonggang Wang, and Hideki Kobayashi, RagA, an mTORC1 activator, interacts with a hedgehog signaling protein, WDR35/IFT121, Genes to Cells,, 24, 2, 151-161, 2019.02, [URL].
4. Takashi Ishiia, Hiroshi Hayakawaa, Tatsuhiro Igawa, Takeshi Sekiguchi and Mutsuo Sekiguchi, Specific binding of PCBP1 to heavily oxidized RNA to induce cell death., PNAS, , 115, 26, 6715-6720, 2018.06.
5. M. K. A Rosli, P. Abdul-Patah, S. M. F. Syed-Shabthar, M. N. Burhanuddin, Takeshi Sekiguchi, Hiroshi Sasaki, M. N. Shukor, S. Yaakop, B. M. Md-Zain, PHYLOGENETIC RELATIONSHIPS OF THE MALAY PENINSULA OTTERS (LUTRA SUMATRANA,LUTROGALE PERSPICILLATA, AND AONYX CINEREUS) BASED ON DNA SEQUENCES OF MITOCHONDRIAL D-LOOP REGION, The Journal of Animal & Plant Sciences, 25, 836-843, 2015.06.
6. Takashi Ishii, Hiroshi Hayakawa, Takeshi Sekiguchi, Noritaka Adachi, Mutsuo Sekiguchi, Role of Auf1 in elimination of oxidatively damaged messenger RNA in human cells., Free Radical Biology and Medicine, 10.1016/j.freeradbiomed.2014.11.018, 79, 109-116, 2015.02, In aerobically growing cells, in which reactive oxygen species are produced, the guanine base of RNA is oxidized to 8-oxo-7,8-dihydroguanine, which induces alterations in gene expression. Here we show that the human Auf1 protein, also called HNRNPD, binds specifically to RNA containing this oxidized base and may be involved in cellular processes associated with managing the problems caused by RNA oxidation. Auf1-deficient cells were constructed from human HeLa and Nalm-6 lines using two different targeting procedures. Both types of Auf1-deficient cells are viable, but exhibit growth retardation. The stability of messenger RNA for four different housekeeping genes was determined in Auf1-deficient and -proficient cells, treated with or without hydrogen peroxide. The level of oxidized messenger RNA was considerably higher in Auf1-deficient cells than in Auf1-proficient cells. Auf1 may play a role in the elimination of oxidized RNA, which is required for the maintenance of proper gene expression under conditions of oxidative stress..
7. Yoko Okawara, Takeshi Sekiguchi, Aya Ikeda, Shingo Miura, Hiroshi Sasaki, Takeshi Fujii, Yayoi Kaneko, Food habits of the urban Japanese weasels Mustela itatsi revealed by faecal DNA analysis, Mammal Study,, 39, 3, 155-161, 2014.09.
8. Takeshi Sekiguchi, Yoshiaki Kamada, Nobuaki Furuno, Minoru Funakoshi, Hideki Kobayashi, Amino acid residues required for Gtr1p-Gtr2p complex formation and its interactions with the Ego1p-Ego3p complex and TORC1 components in yeast, Genes to cells, 19, 6, 449-463, 2014.06, The yeast Ras-like GTPases Gtr1p and Gtr2p form a heterodimer, are implicated in the regulation of TOR complex 1 (TORC1), and play pivotal roles in cell growth. Gtr1p and Gtr2p bind Ego1p and Ego3p, which are tethered to the endosomal and vacuolar membranes where TORC1 functions are regulated through a relay of amino acid signaling interactions. The mechanisms by which Gtr1p and Gtr2p activate TORC1 remain obscure. We probed the interactions of the Gtr1p-Gtr2p complex with the Ego1p-Ego3p complex and TORC1 subunits. Mutations in the region (179-220 a.a.) following the nucleotide-binding region of Gtr1p and Gtr2p abrogated their mutual interaction and resulted in a loss in function, suggesting that complex formation between Gtr1p and Gtr2p was indispensable for TORC1 function. A modified yeast two-hybrid assay revealed that Gtr1p-Gtr2p complex formation is important for its interaction with the Ego1p-Ego3p complex. GTP-bound Gtr1p interacted with the region containing the HEAT repeats of Kog1p and the C-terminal region of Tco89p. The GTP-bound Gtr2p suppressed a Kog1p mutation. Our findings indicate that the interactions of the Gtr1p-Gtr2p complex with the Ego1p-Ego3p complex and TORC1 components Kog1p and Tco89p play a role in TORC1 function..
9. M. K. A. Rosli, S. M. F. Syed-Shabthar, P. Abdul-Patah, Z. Abdul-Samad, S. N. Abdul, M. N. Burhanuddin, N. A. Zulkifli, M. N. Shukor, K. Budsabong, S. Changtragoon, Takeshi Sekiguchi, H. Sasaki, B. M. Md-Zain, A New Subspecies Identification and Population Study of the Asian Small-clawed Otter (Aonyx cinereus) in the Malay Peninsula and Southern Thailand Based on Fecal DNA Method., The Scientific World Journal, 10.1155/2014/457350, 2014, 1-11, 2014.03, [URL].
10. Takashi Ishii, Minoru Funakoshi, Hideki Kobayashi, Takeshi Sekiguchi, Yeast Irc22 Is a Novel Dsk2-Interacting Protein that Is Involved in Salt Tolerance. , Cells, 10.3390/cells3020180, 3, 2, 180-198, 2014.03, [URL].
11. Hachiro Inokuchi, Riyoko Ito, Takeshi Sekiguchi, Mutsuo Sekiguchi, Search for Proteins Required for Accurate Gene Expression under Oxidative Stress: ROLES OF GUANYLATE KINASE AND RNA POLYMERASE., J Biol Chem., 10.1074/jbc.M113.507772, 288, 46, 32952-32962, 2013.11, In aerobically growing cells, in which reactive oxygen species are produced, the guanine base is oxidized to 8-oxo-7,8-dihydroguanine, which can pair with adenine as well as cytosine. This mispairing causes alterations in gene expression, and cells possess mechanisms to prevent such outcomes. In Escherichia coli, 8-oxo-7,8-dihydroguanine-related phenotypic suppression of lacZ amber is enhanced by mutations in genes related to the prevention of abnormal protein synthesis under oxidative stress. A genome-wide search for the genes responsible, followed by DNA sequence determination, revealed that specific amino acid changes in guanylate kinase and in the β and β' subunits of RNA polymerase cause elevated levels of phenotypic suppression, specifically under aerobic conditions. The involvement of the DnaB, DnaN, and MsbA proteins, which are involved in DNA replication and in preserving the membrane structure, was also noted. Interactions of these proteins with each other and also with other molecules may be important for preventing errors in gene expression..
12. Takeshi Sekiguchi, Riyoko Itoh, Hiroshi Hayakawa, Mutsuo Sekiguchi, Elimination and utilization of oxidized Guanine nucleotides in the synthesis of RNA and its precursors., J Biol Chem. , doi: 10.1074/jbc.M112.418723. , 288, 12, 8128-8135, 2013.03.
13. Sekiguchi, T., Sasaki, T., Funakoshi, M., Ishii, T., Saitoh, Y., Kaneko, S., Kobayashi, H, Ubiquitin chains in the DSK2 UBL domain mediate DSK2 stability and protein degradation in Yeast, Biochem. Biophys. Res. Commun., 411, 3, 555-561, 2011.08.
14. T. Sekiguchi, H. Sasaki, Y. Kurihara, S. Watanabe, D. Moriyama, N. Kurose, R. Matsuki, K. Yamazaki and M. Saeki, New methods for species and sex determination in three sympatric Mustelids, Mustela itatsi, Mustela sibirica, and Martes melampus , Molecular Ecology Resources, 10, 6, 1089-1091, 2010.10.
15. Wang, YG., Kurihara, Y., Sato, T., Toh, H., Kobayashi, H. and Sekiguchi, T. , The Gtr1p associated with Gtr2p and with Ego1p differently, Gene, 437, 32-38, 2009.05, [URL].
16. Yukiko Horiike, Hideki Kobayashi, Takeshi Sekiguchi, Ran GTPase guanine nucleotide exchange factor RCC1 is phosphorylated on serine 11 by cdc2 kinase in vitro, Molecular biology reports, 36, 717, 2009.03, [URL].
17. Sekiguchi, T., Hayashi, N., Wang, Y., Kobayashi, H., Genetic evidence that Ras-like GTPases, Gtr1p and Gtr2p, are involved in epigenetic control of gene expression in Saccharomyces cerevisiae, Biochem Biophys Res Commun, 368, 3, 748-754, 2008.04.
18. Sekiguchi, T., Kurihara, Y., Fukumura, J. , Phosphorylation of Threonine 204 of DEAD-BOX RNA helicase DDX3 by cyclin B/cdc2 in vitro. , Biochem. Biophys. Res. Commun. , 356, 668-673, 2007.05.
19. Sekiguchi1,T., Hayano,T., Yanagida, M., Takahashi,N., Nishimoto,T., NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47., Nucleic Acid Res., 34,4593-4608, 2006.09.
20. Yonggang Wang, Nobutaka Nakashima, Takeshi Sekiguchi and Takeharu Nishimoto, Saccharomyces cerevisiae GTPase complex: Gtr1p-Gtr2p, regulates cell-proliferation through Saccharomyces cerevisiae Ran-binding protein, Yrb2p, Biochemical and Biophysical Research Communications, 10.1016/j.bbrc.2005.08.108, 336, 2, 639-645, 336,639-645, 2005.01.
21. Yuko Todaka, Yonggang Wang, Kosuke Tashiro, Nobutaka Nakashima Takeharu Nishimoto and Takeshi Sekiguchi, Association of GTP binding protein Gtr1p with Rpc19p, a sharedsubunit of RNA polymerase I and III in yeast Saccharomyces cerevisiae., Genetics, 170,1515-1524, 2005.01.
22. Sekiguchi, T., Iida, H., Fukumura, J. and Nishimoto T, Human DDX3Y, the Y-encoded isoform of RNA helicase DDX3, rescues a hamster temperature-sensitive ET24 mutant cell line with a DDX3X mutation., Exp. Cell. Res., 10.1016/j.yexcr.2004.07.005, 300, 1, 213-222, Vol.300 pp213-222, 2004.10.
23. Sekiguchi, T., Todaka Y., Wang YG., Hirose, E., Nakashima, N. and Nishimoto, T., A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D., J. Biol. Chem., 10.1074/jbc.M305935200, 279, 9, 8343-8350, Vol.279 pp8343-8350, 2004.01.
24. Wang, YG., Sekiguchi, T., Noguchi T., and Nishimoto T., A hamster temperature-sensitive alanyl-tRNA synthetase mutant
causes degradation of cell-cycle related proteins and apoptosis, J Biochem (Tokyo), 10.1093/jb/mvh001, 135, 1, 7-16, Vol.135 pp7-16, 2004.01.
25. Fukumura, J., Noguchi, E., Sekiguchi, T., and Nishimoto, T., A temperature-sensitive mutant of the mammalian RNA helicase,
DEAD-BOX X isoform, DBX, defective in the transition from G1 to S phase, J Biochem (Tokyo), 10.1093/jb/mvg126, 134, 1, 71-82, Vol.134, pp71-82, 2003.07.
26. Sekiguchi, T., Hirose, E., Nakashima, N., Ii, M. and Nishimoto, T., Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins Rag A and Rag B., J. Biol. Chem., 10.1074/jbc.M004389200, 276, 10, 7246-7257, Vol.276,No.10,pp.7246-7257, 2001.01.
27. Yoshimi, M, Sekiguchi, T, Hara, N and T, Nishimoto ., Inhibition of N-linked glycosylation causes apoptosis in hamster BHK21 cells., Biochem. Biophys. Res. Commun., 10.1006/bbrc.2000.3565, 276, 3, 965-969, Vol.276, pp965-969, 2000.01.
28. T, Sekiguchi, T.Nishimoto and T. Hunter, Overexpression of D-type cyclins, E2F-1, SV40 large T antigen and HPV16 E7 rescue cell cycle arrest of tsBN462 cells caused by the CCG1/TAFII250 mutation, Oncogene., 10.1038/sj.onc.1202508, 18, 10, 1797-1806, Vol.18,pp.1797-1806, 1999.03.
29. Hirose, E., Nakashima, N., Sekiguchi, T.and T.Nishimoto., RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway, J. Cell Sci., 111, 11-21, Vol.111,No.1,pp.11-21, 1998.01.
30. Sekiguchi, T., T. Hunter, Induction of growth arrest and cell death by overexpression of the cyclin-Cdk inhibitor p21 in hamster BHK21 cells, Oncogene., Vol.16,pp.369-380, 1998.01.
31. Sekiguchi, T., Hayashida, T., Nakashima, T., Toyoshima, H., Nishimoto, T and T. Hunter.., D-type cyclin expression is decreased and p21 and p27 CDK inhibitor expression is increased when tsBN462 CCG1/TAFII250 mutant cells arrest in G1 at the restrictive temperature, Genes Cells., 10.1046/j.1365-2443.1996.00259.x, 1, 7, 687-705, Vol.1,No.7,pp.687-705, 1996.07.
32. T.Sekiguchi, T. Nakashima, T. Hayashida, A. Kuraoka, S. Hashimoto, N. Tsuchida, Y. Shibata, T. Hunter, and T. Nishimoto, Apoptosis is induced in BHK cells by the tsBN462/13 mutation in the CCG1/TAF250 subunit of the TFIID basal transcription factor, Exp. Cell Res., 10.1006/excr.1995.1183, 218, 2, 490-498, Vol.218,No.2,pp.490-498, 1995.02.
33. Noguchi E; Sekiguchi T; Nohiro Y; Hayashida T; Hirose E; Hayashi N and T. Nishimoto., Minimum essential region of CCG1/TAFII250 required for complementing the temperature-sensitive cell cycle mutants, tsBN462 and ts13 cells, of hamster BHK21 cells, Somat. Cell Mol. Genet., 10.1007/BF02255841, 20, 6, 505-513, Vol.20,No.6,pp.505-13, 1994.06.
34. Miyabashira J., Sekiguchi, T., and Nishimoto T., Mammalian cells have two functional RCC1 proteins produced by alternative splicing, J. Cell Sci., 107, 2203-2208, Vol.107,No.8,pp.2203-8, 1994.08.
35. Nakashima T; Sekiguchi T; Sunamoto H; Yura K; Tomoda S; Go M; Kere J; Schlessinger D; Nishimoto T., Structure of the human CCG1 gene: relationship between the exons/introns and functional domain/modules of the protein, Gene, 141, 2, 193-200, Vol.141,No.2,pp.193-200, 1994.02.
36. Hayashida T; Sekiguchi T; Noguchi E; Sunamoto H; Ohba T; Nishimoto T., The CCG1/TAFII250 gene is mutated in thermosensitive G1 mutants of the BHK21 cell line derived from golden hamster, Gene, 141, 2, 267-270, Vol.141,No.2,pp.267-70, 1994.02.
37. Nakashima T; Masuda A; Sekiguchi T and Nishimoto T and Uemura T, Preliminary findings of chromosomal alterations and expression of
cell cycle genes in head and neck tumors., EUROPEAN ARCHIVES OF OTO-RHINO-LARYNGOLOGY., 10.1007/BF02565228, 251, S87-S90, Vol.251 (S1) S87-S90., 1994.01.
38. Noguchi E; Sekiguchi T; Yamashita K; Nishimoto T., Molecular cloning and identification of two types of hamster cyclin-dependent
kinases: cdk2 and cdk2L., Biochem. Biophys. Res. Com,, Vol.197 (3) pp1524-9., 1993.03.
39. Nakashima T; Sekiguchi T; Kuraoka A; Fukushima K; Shibata Y; Komiyama S; Nishimoto T, Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose defect causes apoptotic cell death in hamster BHK21 cells., Mol. Cell. Biol., 13, 10, 6367-6374, Vol.13,No.10,pp.6367-74, 1993.10.
40. Seino,H. Hisamoto,N. Uzawa,S. Sekiguchi,T. and T.Nishimoto., DNA-binding domain of RCC1 protein is not essential for coupling mitosis
with DNA replication., Journal of Cell Science., 102, 393-&, Vol.102 pp393-400., 1992.01.
41. Watanabe,M. Furuno,N. Goebl,M. Go,M. Miyauchi,K. Sekiguchi,T., Molecular cloning of the human gene, CCG2, that complements the BHK-derived temperature-sensitive cell cycle mutant tsBN63: identity of CCG2 with the human X chromosomal, Journal of Cell Science., Vol.100 pp35-43., 1991.01.
42. Seino,H. Nishitani,H. Seki,T. Hisamoto,N. Tazunoki,T. Shiraki,N. Ohtsubo,M. Yamashita,K. Sekiguchi,T. and T.Nishimoto., RCC1 is a nuclear protein required for coupling activation of cdc2 kinase with DNA synthesis and for start of the cell cycle., Cold Spring Harbor Symposia on Quantitative Biology, 56, 367-375, Vol.LVI. pp367-375., 1991.01.
43. Sekiguchi,T., Nohiro,Y., Nakamura,Y., Hisamoto,N.and T.Nishimoto., The human CCG1 gene, essential for progression of the G1 phase, encodes a 210-Kilodalton nuclear DNA-binding protein, Molecular and Cellular Biology., 11, 6, 3317-3325, Vol.11,pp.3317-3325, 1991.11.
44. Uchida,S., Sekiguchi,T., Nishitani,H., Miyauchi,K., Ohtsubo,M.and T.Nishimoto., Premature chromosome condensation is induced by a point mutation in the hamster RCC1 gene, Molecular and Cellular Biology., 10, 2, 577-584, Vol.10,pp.577-584, 1990.10.
45. Brown,C.J. Sekiguchi,T. Nishimoto,T. and H.F.Willard, Regional localization of CCG1 gene which complements hamster cell cycle
mutation BN462 to Xq11-Xq13., Somatic Cell and Molecular Genetics., 10.1007/BF01534674, 15, 1, 93-96, Vol.15 pp93-96.9.S10., 1989.01.
46. Sekiguchi,T., Miyata,T.and T.Nishimoto., Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the BHK cell line, The EMBO Journal., 7, 6, 1683-1687, Vol.7,pp.1683-1687, 1988.01.
47. Ohtsubo,M. Kai,R. Furuno,N. Sekiguchi,T. Sekiguchi,M. Hayashida,H. Miyata,T. Fukushige,S. Murotsu,T. Matsubara,K. and T.Nishimoto., Isolation and characterization of the active cDNA of
the human cell cycle gene(RCC1) involved in the regulation of onset of
chromosome condensation., Gene & Development, 10.1101/gad.1.6.585, 1, 6, 585-593, Vol.1 pp585-593., 1987.01.
48. Sekigcuhi, T. Yoshida, M.C. Sekiguchi, M. and T.Nishimoto.., Isolation of a human X chromosome-linked gene essential for progression from G1 to S phase of the cell cycle, Experimental Cell Research., 10.1016/0014-4827(87)90200-X, 169, 2, 395-407, Vol.169,pp.395-407, 1987.01.
49. Transformation of temperature-sensitive growth mutant of BHK21 cell line to wild-type phenotype with hamster and mouse DNA..
50. Sekiguchi,T. Nishimoto,T. Kai,R. and M.Sekiguchi., Recovery of hybrid vector, derived from bovine papilloma virus DNA, pBR322 and the
HSVtk gene, by bacterial transformation with extrachromosomal DNA from
transfected rodent cells., Gene., 21, 3, 267-272, Vol.21 pp267-272., 1983.01.
51. Nishimoto,T. Sekiguchi,T. Kai,R. Yamashita,K. Takahashi,T. and M, Sekiguchi, Large-scale selection and analysis of
temperature-sensitive mutants for cell reproduction from BHK cells., Somatic Cell Genetics., 10.1007/BF01543021, 8, 6, 811-824, Vol.8 pp811-824., 1982.01.