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Publication

2017

2016

2015

  • Reincke, M., Sbiera, S., Hayakawa, A., Theodoropoulou, M., Osswald, A., Beuschlein, F., Meitinger, T., Mizuno-Yamasaki, E., Kawaguchi, K., Saeki, Y., Tanaka, K., Wieland, T., Graf, E., Saeger, W., Ronchi, C.L., Allolio, B., Buchfelder, M., Strom, T.M., Fassnacht, M., and Komada, M. (2015) Mutations in the deubiquitinase gene USP8 cause Cushing's disease. Nat. Genet. 47, 31-38
  • Perez-Rivas, L.G., Theodoropoulou, M., Ferrau, F., Nusser, C., Kawaguchi, K., Stratakis, C.A., Reuda Faucz, F., Wildemberg, L.E., Assie, G., Beschorner, R., Dimopoulou, C., Buchfelder, M., Popovic, V., Berr, C.M., Toth, M., Ardisasmita, A.I., Honegger, J., Bertherat, J., Gadelha, M.R., Beuschlein, F., Stalla, G., Komada, M., Korbonits, M., and Reincke, M. (2015) The gene of the ubiquitin-specific protease 8 is frequently mutated in adenomas causing Cushing's disease. J. Clin. Endocrinol. Metab. 100, E997-E1004 (Chosen as the cover image of the issue)
  • *Theodoropoulou, M., Reincke, M., Fassnacht, M., and *Komada, M. (*co-correspondence) (2015) Decoding the genetic basis of Cushing's disease: USP8 in the spotlight. Eur. J. Endocrinol. 173, M73-M83
  • Sun, X.-X., He, X., Yin, L., Komada, M., Sears, R.C., and Dai, M.-S. (2015) The nucleolar ubiquitin-specific protease USP36 deubiquitinates and stabilizes c-Myc. Proc. Natl. Acad. Sci. USA 112, 3734-3739
  • 駒田雅之 (2015) 脱ユビキチン化酵素USP8の機能獲得型変異はCushing病をひき起こす. ライフサイエンス新着論文レビュー ”First Author's"
  • 川口紘平、駒田雅之 (2015) 見えてきたユビキチンを介した核小体の多彩な機能ファルマシア 51, 300-304
  • 川口紘平、駒田雅之 (2015) 難病 ”クッシング病” 発症の分子メカニズム. バイオサイエンスとインダストリー 73, 300-301
  • 駒田雅之 (2015) 脱ユビキチン化酵素USP8の機能獲得型変異がクッシング病を引き起こす. ACTH Related Peptides 26, 56-58
  • 駒田雅之 (2015) 脱ユビキチン化酵素USP8変異とCushing病. クッシング症候群診療マニュアル, 259-260

 

2014

  • *Tanno, H., *Shigematsu, T. (*equal contribution), Nishikawa, S., Hayakawa, A., Denda, K., Tanaka, T., and Komada, M. (2014) Ubiquitin-interacting motifs confer full catalytic activity, but not ubiquitin chain substrate specificity, to deubiquitinating enzyme USP37. J. Biol. Chem. 289, 2415-2423
  • Le Bras, B., Freal, A., Czarnecki, A., Legendre, P., Bullier, E., Komada, M, Brophy P.J., Davenne, M., and Couraud, F. (2014) In vivo assembly of the axon initial segment in motor neurons. Brain Struct. Funct. 219, 1433-1450

 

2013

  • Li, X., Bian, Y., Takizawa, Y., Hashimoto, T., Ikoma, T., Tanaka, J., Kitamura, N., Inagaki, Y., Komada, M., and Tanaka, T. (2013) ERK-dependent downregulation of Skp2 reduces Myc activity with HGF, leading to inhibition of cell proliferation through a decrease in Id1 expression. Mol. Cancer Res.11, 1437-1447
  • Tanno, H. and Komada, M. (2013) The ubiquitin code and its decoding machinery in the endocytic pathway. J. Biochem. 153, 497-504
  • Terada, N., Saitoh, Y., Ohno, N., Komada, M., Yamauchi, J., and Ohno, S. (2013) Involvement of Src in the membrane skeletal complex, MPP6-4.1G, in Schmidt-Lanterman incisures of mouse myelinated nerve fibers in PNS. Histochem. Cell Biol. 140, 213-222
  • Daocharad Burana、後藤聡、駒田雅之 (2013) ユビキチン化によるFrizzledのリソソーム分解を介したWntシグナル強度の制御. 細胞工学 特集「Wnt協奏曲」32, 396-400

 

2012

  • Mukai, A., Yamamoto-Hino, M., Komada, M., Okano, H., and Goto, S. (2012) Balanced ubiquitination determines cellular responsiveness to extracellular stimuli. Cell. Mol. Life Sci. 69, 4007-4016
  • Tanno, H., Yamaguchi, T., Goto, E., Ishido, S., and Komada, M. (2012) The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. Mol. Biol. Cell 23, 1343-1353
  • Terada, N., Saitoh, Y., Ohno, N., Komada, M., Saitoh, S., Peles, E., and Ohno, S. (2012) Essential function of protein 4.1G in targeting of MPP6 into Schmidt-Lanterman incisures in myelinated nerves. Mol. Cell. Biol. 32, 199-205

 

2011

  • Denda, K., Nakao-Wakabayashi, K., Okamoto, N., Kitamura, N., Ryu, J.-Y., Tagawa, Y., Ichisaka, T., Yamanaka, S., and Komada, M. (2011) Nrk, an X-linked protein kinase in the germinal center kinase family, is required for placental development and fetoplacental induction of labor. J. Biol. Chem. 286, 28802-28810
  • Hanafusa, H., Ishikawa, K., Kedashiro, S., Saigo, T., Iemura, S., Natsume, T., Komada, M., Shibuya, H., Nara, A., and Matsumoto, K. (2011) Leucine-rich repeat kinase LRRK1 regulates endosomal trafficking of the EGF receptor. Nat. Commun. 2, 158
  • 駒田雅之 (2011) ユビキチン化による核小体の構造と機能の制御. 生体の科学 特集 「細胞核 - 構造と機能」 62, 422-423
  • 駒田雅之 (2011) ンドサイトーシス」, 「FYVE ドメイン」生化学事典 (印刷中) 

 

2010

  • Mukai, A., Yamamoto-Hino, M., Awano, W., Watanabe, W., *Komada, M., and *Goto, S. (*co-correspondence) (2010) Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt. EMBO J. 29, 2114-2125(Picked up in “Have you seen?”: Cadigan, K.M. (2010) Receptor endocytosis: Frizzled joins the ubiquitin club. EMBO J. 29, 2099-2100)
  • Saitsu, H., Tohyama, J., Kumada, T., Egawa, K., Hamada, K., Okada, I., Mizuguchi, T., Osaka, H., Miyata, R., Furukawa, T., Haginoya, K., Hoshino, H., Goto, T., Hachiya, Y., Yamagata, T., Saitoh, S., Nagai, T., Nishiyama, K., Nishimura, A., Miyake, N., Komada, M., Hayashi, K., Hirai, S., Ogata, K., Kato, M., Fukuda, A., and Matsumoto, N. (2010) Dominant-negative mutations in α-II spectrin cause West syndrome with severe cerebral hypomyelination, spastic quadriplegia, and developmental delay. Am. J. Hum. Genet. 86, 881-891
  • Howell, O.W., Rundle, J.L., Garg, A., Komada, M., Brophy, P.J., and Reynolds, R. (2010) Activated microglia mediate axo-glial disruption that contributes to axonal injury in multiple sclerosis. J. Neuropathol. Exp. Neurol. 69,1017-1033
  • Terada, N., Ohno, N., Saitoh, S., Saitoh, Y., Komada, M., Kubota, H., and Ohno, S. (2010) Involvement of a membrane skeletal protein, 4.1G, for Sertoli/germ cell interaction. Reproduction 139, 883-892
  • 駒田雅之、後藤聡 (2010) 受容体のユビキチン化と脱ユビキチン化を介した細胞のWnt応答性の制御. 細胞工学 特集「拡大するユビキチンバイオロジー」29, 1237-1243
  • 駒田雅之、遠藤彬則 (2010) 脱ユビキチン化酵素群の細胞機能. 生化学(総説) 82, 378-387
  • 駒田雅之 (2010) 軸索に特異的なスペクトリン細胞膜骨格の機能. 生体の科学 特集「シナプスをめぐるシグナリング」61, 498-499

 

2009

  • Endo, A., Matsumoto, M., Inada, T., Yamamoto, A., Nakayama, K.I., Kitamura, N., and Komada, M. (2009) Nucleolar structure and function are regulated by the deubiquitylating enzyme USP36. J. Cell Sci. 122, 678-686 (Chosen as the cover image of the issue, Picked up in “In This Issue”: J. Cell Sci. 122, e501)
  • Endo, A., Kitamura, N., and Komada, M. (2009) Nucleophosmin/B23 regulates ubiquitin dynamics in nucleoli by recruiting deubiquitylating enzyme USP36. J. Biol. Chem. 284, 27918-27923
  • Ohno, N., Terada, N., Komada, M., Saitoh, S., Costantini, F., Pace, V., Germann, P.G., Weber, K., Yamakawa, H., Ohara, O., and Ohno, S. (2009) Dispensable role of protein 4.1B/DAL-1 in rodent adrenal medulla regarding generation of pheochromocytoma and plasmalemmal localization of TSLC1. Biochim. Biophys. Acta 1793, 506-515
  • 駒田雅之、遠藤彬則 (2009) 核小体の機能のユビキチンダイナミクスによる制御. 生体の科学 特集 「ユビキチン化による生体機能の調節」 60, 521-526
  • 駒田雅之、向井明子 (2009) ユビキチン修飾系による細胞質分裂の制御. 蛋白質核酸酵素 (Review) 54, 11-19
  • 駒田雅之 (2009) 増殖因子受容体の分解制御と制癌 in バイオ研究のフロンティア3−医療・診断をめざす先端バイオテクノロジー, pp 59-66 (関根光雄 編、工学図書)

 

2008

  • Mukai, A., Mizuno, E., Kobayashi, K., Matsumoto, M., Nakayama, K.I., Kitamura, N., and Komada, M. (2008) Dynamic regulation of ubiquitylation and deubiquitylation at the central spindle during cytokinesis. J. Cell Sci. 121, 1325-1333
  • Sato, Y., Yoshikawa, A., Yamagata, A., Mimura, H., Yamashita, M., Ookata, K., Nureki, O., Iwai, K., Komada, M., and Fukai, S. (2008) Structural basis for selective cleavage of Lys63-linked polyubiquitin chains. Nature (article) 455, 358-362
  • Nakagawa, H., Tamura, A., Wakabayashi, K., Hoshijima, K., Komada, M., Yoshida, T., Kometani, S., Matsubara, T., Mikuriya, K., and Ishikawa, T. (2008) Ubiquitin-mediated proteasomal degradation of non-synonymous SNP variants of human ABC transporter ABCG2. Biochem. J. 411, 623-631
  • Kosaka, T., Komada, M., and Kosaka, K. (2008) Sodium channel cluster, βIV-spectrin and ankyrinG positive "hot spots" on dendritic segments of parvalbumin-containing neurons and some other neurons in the mouse and rat main olfactory bulbs. Neurosci. Res. 62, 176-186
  • Komada, M. (2008) Controlling receptor downregulation by ubiquitination and deubiquitination. Curr. Drug Discov. Technol. 5, 78-84 (Invited Review)
  • 向井明子、駒田雅之 (2008) エンドソームと細胞質分裂の接点−ユビキチン化/脱ユビキチン化による調節. 蛋白質核酸酵素 増刊号 「メンブレントラフィックの奔流」53, 2094-2098

 

2007

  • Uemoto, Y., Suzuki, S., Terada, N., Ohno, N., Ohno, S., Yamanaka, S., and Komada, M. (2007) Specific role of the truncated βIV-spectrin Σ6 in sodium channel clustering at axon initial segments and nodes of Ranvier. J. Biol. Chem. 282, 6548-6555
  • Mizuno, E., Kitamura, N., and Komada, M. (2007) 14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and its cancellation in the M phase. Exp. Cell Res. 313, 3624-3634 (Picked up in “Highlights”: Exp. Cell Res. 313 (16), pages v-vi)
  • Wakabayashi, K., Nakagawa, H., Tamura, A., Koshiba, S., Hoshijima, K., Komada, M., and Ishikawa, T. (2007) Intramolecular disulfide bond is a critical checkpoint determining degradative fates of ATP- binding cassette (ABC) transporter ABCG2 protein. J. Biol. Chem. 282, 27841-27846
  • Nishimura, K., Akiyama, H., Komada, M., and Kamiguchi, H. (2007) βIV-spectrin forms a diffusion barrier against L1CAM at the axon initial segment. Mol. Cell. Neurosci. 34, 422-430
  • Terada, N., Ohno, N., Saitoh, S., Seki, G., Komada, M., Suzuki, T., Yamakawa, H., Soleimani, M., and Ohno, S. (2007) Interaction of membrane skeletal protein, protein 4.1B and p55, and sodium bicarbonate cotransporter 1 in mouse renal S1-S2 proximal tubues. J. Histochem. Cytochem. 55, 1199-1206
  • Komada, M. (2007) Regulation of endosomal cargo sorting by deubiquitinating enzymes. In Research Advances in Biological Chemistry R.M. Mohan, eds. (Kerala, India: Global Research Network), pp.27-38 (Invited Review)
  • 寺田信生、大野伸彦、駒田雅之、大野伸一 (2007) 神経繊維ランビエ絞輪部近傍の軸索構築に関するタンパク質間相互作用. 生体の科学 特集 「タンパク質間相互作用」 58, 476-477

 

2006

  • Yamasaki, A., Tani, K., Yamamoto, A., Kitamura, N., and Komada, M. (2006) The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A. Mol. Biol. Cell 17, 4876-4887(Picked up in ‘Faculty of 1000 Biology' )
  • Mizuno, E., Kobayashi, K., Yamamoto, A., Kitamura, N., and Komada, M. (2006) A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 7, 1017-1031
  • Nakamura, N., Tanaka, N., Kitamura, N., and Komada, M. (2006) Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes. Genes Cells 11, 593-606
  • Ohno, N., Terada, N., Yamakawa, H., Komada, M., Ohara, O., Trapp, B.D., and Ohno, S. (2006) Expression of protein 4.1G in Schwann cells of the peripheral nervous system. J. Neurosci. Res. 84, 568-577
  • 駒田雅之、水野英美 (2006) エンドソームにおけるメンブレントラフィックの脱ユビキチン化による調節. 細胞工学 特集 「メンブレントラフィック研究の新局面」 11, 1258-1263

 

2005

  • Mizuno, E., Iura, T., Mukai, A., Yoshimori, T, Kitamura, N., and Komada, M. (2005) Regulation of epidermal growth factor receptor downregulation by UBPY-mediated deubiquitination at endosomes. Mol. Biol. Cell 16, 5163-5174
  • Komada, M. and Kitamura, N. (2005) The Hrs/STAM complex in the downregulation of receptor tyrosine kinases. J. Biochem. 137, 1-8 (Invited Review) (Chosen as the cover image of the issue.)
  • 駒田雅之 (2005) 軸索起始部とランビエ絞輪へのNaチャネル局在化機構. 生体の科学 特集 「Naチャネル」 56, 221-225

 

2004

  • Mizuno, E., Kawahata, K., Okamoto, A., Kitamura, N., and Komada, M. (2004) Association with Hrs is required for the early endosomal localization, stability, and function of STAM. J. Biochem. 135, 385-396 (Chosen as the cover image of the issue, 平成17年度J. Biochem. 論文賞)
  • Morino, C., Kato, M., Yamamoto, A., Hayakawa, A., Mizuno, E., Komada, M., and Kitamura, N. (2004) A role for Hrs in endosomal sorting of ligand-stimulated and unstimulated epidermal growth factor receptor. Exp. Cell Res. 297, 380-391
  • 駒田雅之 (2004) 受容体チロシンキナーゼのユビキチン化による分解機構. 現代医療 36, 879-885
  • 駒田雅之 (2004) ホスファチジルイノシトール3-リン酸とエンドソームにおける膜輸送. ファルマシア 40, 635-639

 

2003

  • Mizuno, E., Kawahata, K., Kato, M., Kitamura, N., and Komada, M. (2003) STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif. Mol. Biol. Cell 14, 3675-3689
  • Kunzmann, S., Wohlfahrt, J.G., Itoh, S., Asao, H., Komada, M., Akdis, C.A., Blaser, K., and Schmidt-Weber, C.B. (2003) SARA and Hgs attenuate susceptibility to TGF-β1-mediated T cell suppression. FASEB J. 17, 194-202

 

~2002(代表的な論文)

  • Komada, M. and Soriano, P. (2002) βIV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier. J. Cell Biol. 156, 337-348
  • Komada, M. and Kitamura, N. (2001) Hrs and Hbp: possible regulators of endocytosis and exocytosis. Biochem. Biophys. Res. Commun. 281, 1065-1069 (Invited Review)
  • Komada, M., McLean, D.J., Griswold, M.D., Russell, L.D., and Soriano, P. (2000) E-MAP-115, encoding a microtubule-associated protein, is a retinoic acid-inducible gene required for spermatogenesis. Genes Dev. 14, 1332-1342
  • Komada, M. and Soriano, P. (1999) Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis. Genes Dev. 13, 1475-1485
  • Komada, M., Masaki, R., Yamamoto, A., and Kitamura, N. (1997) Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes. J. Biol. Chem. 272, 20538-20544
  • Komada, M. and Kitamura, N. (1995) Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally conserved putative zinc finger domain. Mol. Cell. Biol. 15, 6213-6221
  • Komada, M. and Kitamura, N. (1994) Regulatory role of major tyrosine autophosphorylation site of kinase domain of c-Met receptor (scatter factor/hepatocyte growth factor receptor). J. Biol. Chem. 269, 16131-16136
  • Komada, M. and Kitamura, N. (1993) The cell dissociation and motility triggered by scatter factor/hepatocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor. Oncogene 8, 2381-2390