Identification of novel AKT regulating molecules.

• Project/Area Number: 19770098
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Single-year Grants
• Research Field: Functional biochemistry
• Research Institution: Hokkaido University
• Principal Investigator: SUIZU Futoshi Hokkaido University, 遺伝子病制御研究所, 助教 (90431379)
• Project Period (FY): 2007 – 2009
• Project Status: Completed (Fiscal Year 2009)
• Budget Amount: ¥3,750,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥450,000); Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000); Fiscal Year 2008: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000); Fiscal Year 2007: ¥1,800,000 (Direct Cost: ¥1,800,000)
• Keywords: タンパク分解 / リン酸化 / AKT / ユビキチン / セリンスレオニンキナーゼ / ダウン症 / 21Trisomy / TTC3

Research Abstract

In yeast two-hybrid assays, we found that TTC3, which is located at chromosome 21 within the Down Syndrome Critical Region, specifically interacted with Akt. TTC3 preferentially binds to phosphorylated Akt and facilitates its ubiquitination/degradation predominantly within the nucleus. By confocal microscopy the TTC3 co-localizes with Akt throughout the cell cycle, suggesting that TTC3 regulate cell survival and proliferation by controlling Akt activity within the nucleus. (Suizu et al. Developmental Cell 2009)

Research Products

• [Journal Article] The E3 Ligase TTC3 Facilitates Ubiquitination and Degragation of Phosphorylated Akt. (2009)
  • Author(s): Suizu, F., Hiramuki, Y., Okumura, F., Matsuda, M., Okumura, A.J., Hirata, N, Narita, M., Kohno, T., Yokota, J., Bohgaki, M., Obuse, C., Hatakeyama, S., Obata, T., Noguchi, M.
  • Journal Title: Developmental Cell 17(6) Pages: 800-810
  • Peer Reviewed
• [Journal Article] The death effector domain-containing DEDD supports S6K1 activity via preventing Cdk1-dependent inhibitory phosphorylation. (2009)
  • Author(s): Kurabe, N., Arai, S., Nishijima, A., Kubota, N., Suizu, F., Mori, M., Kurokawa, J., Miyazaki, M.K., Ide, T., Murakami, K., Ueki, K., Koga, H., Yatomi, Y., Tashiro, F., Noguchi, M., Kadowaki, T., Miyazaki, T.
  • Journal Title: J Biol Chem 284(8) Pages: 5050-5055
  • Peer Reviewed
• [Journal Article] The E3 Ligase TTC3 Facilitates Ubiquitination and Degradation of Phosphorylated Akt (2009)
  • Author(s): Suizu, F.
  • Journal Title: Developmental Cell 17 Pages: 800-810
  • NAID: 120005385335
  • Peer Reviewed
• [Journal Article] The death effector domain-containing DEDD supports S6K1 activity via preventing Cdkl-dependent inhibitory phosphorylation (2009)
  • Author(s): N. Kurabe
  • Journal Title: J. Biol. Chem 284 Pages: 5050-5055
  • Peer Reviewed
• [Journal Article] Regulation of the PI3K-Akt Network: Current Status and a Promise for the Treatment of Human Diseases. (2008)
  • Author(s): Noguchi, M., Obata, T., Suizu, F.
  • Journal Title: Curr Sig Thera 3 Pages: 138-151
  • Peer Reviewed
• [Journal Article] Regulation of the PI3K-Akt Network : Current, Status and a Promise for the Treatment of Human Diseases (2008)
  • Author(s): M. Noguchi
  • Journal Title: Corr Sig. Thera 3 Pages: 138-151
  • Peer Reviewed
• [Journal Article] Regulation of the PI3K-Akt Network: Current Status and a Promise for the Treatment of Human Diseases. (2008)
  • Author(s): M. Noguchi
  • Journal Title: Curr Sig. Thera (In press)
  • Peer Reviewed
• [Journal Article] Protooncogene TCL1: More Than Just a Co-Activator for AKT. (2007)
  • Author(s): Noguchi, M., Ropars, V., Roumestand, C., Suizu, F.
  • Journal Title: FASEB J 21(10) Pages: 2273-2284
  • Peer Reviewed
• [Journal Article] Protooncogene TCL1: More than just as a co-activator for Akt. (2007)
  • Author(s): M. Noguchi
  • Journal Title: FASEB J. 21 Pages: 2273-2284
  • Peer Reviewed
• [Presentation] TTC3 is an E3 logase for Akt that facilitate ubiquitination and degradation of phosphorylated Akt. (2010)
  • Author(s): Suizu, F.
  • Organizer: Keystone Symposia
  • Place of Presentation: Fairmont Hotel, Vancouver
  • Year and Date: 2010-03-13
• [Presentation] TTC3 is an E3 ligase for Akt that facilitates ubiquitination and degradation of phosphorylated Akt (2010)
  • Author(s): 水津太
  • Organizer: Keystone Symposia
  • Place of Presentation: Fairmont Hotel, Vancouver Canada(http://www.igm.hokudai.ac.jp/hu_ifgm_cb/index.html)
  • Year and Date: 2010-03-13
• [Presentation] A novel E3 ligase for Akt facilitates ubiquitination and degradation. (2009)
  • Author(s): 水津太
  • Organizer: 日本分子生物学会
  • Place of Presentation: パシフィコ横浜
  • Year and Date: 2009-12-11
• [Presentation] A novel E3 ligase for Akt that facilitates ubiquitination and degradation of phosphorylated Akt (2009)
  • Author(s): 水津太
  • Organizer: 日本分子生物学会
  • Place of Presentation: パシフィコ横浜・横浜
  • Year and Date: 2009-12-11
• [Presentation] "Akt-in"a peptide inhibitor for AKT, implications for cancer therapy. (2008)
  • Author(s): Noguchi, M.
  • Organizer: AACR
  • Place of Presentation: Hiltone Hotel, Bostone, USA
  • Year and Date: 2008-11-12
• [Presentation] "Akt-in" a peptide inhibitor for AKT, implications for cancer therapy (2008)
  • Author(s): M. Noguchi
  • Organizer: AACR
  • Place of Presentation: ボストン(米)・ヒルトンホテル
  • Year and Date: 2008-11-12
• [Presentation] リンパ系ウイルス感染症におけるPI3K-AKTシグナル伝達系の活性化機構 (2008)
  • Author(s): 野口昌幸
  • Organizer: リンパ網内系学会
  • Place of Presentation: 北海道大学
  • Year and Date: 2008-06-14
• [Presentation] リンパ系ウイルス感染症におけるPI3K-AKTシグナル伝達系の活性化機構 (2008)
  • Author(s): 野口昌幸
  • Organizer: リンパ網内系学会
  • Place of Presentation: 札幌・北海道大学
  • Year and Date: 2008-06-14
• [Presentation] PI3K-AKT network as a Therapeutic Target For Human Disease. (2007)
  • Author(s): Noguchi, M.
  • Organizer: International Drug Discovery Science and Technology(IDDST) 2007
  • Place of Presentation: グランドニューワールドホテル西安(中国)
  • Year and Date: 2007-11-08
• [Presentation] Protooncogene TCL1: More than just a co-activator for Akt. (2007)
  • Author(s): 野口昌幸
  • Organizer: 日本癌学会
  • Place of Presentation: パシフィコ横浜
  • Year and Date: 2007-10-03
• [Remarks]
  • URL: http://www.igm.hokudai.ac.jp/hu_ifgm_cb/index.html
• [Remarks]
  • URL: http://www.igm.hokudai.ac.jp/hu_ifgm_cb/index.html