Tumorigenic transformation by CPI-17 through inhibition of a merlin phosphatase

被引：0
|
作者：
Hongchuan Jin
Tobias Sperka
Peter Herrlich
Helen Morrison
机构：
[1] Leibniz Institute of Age Research–Fritz-Lipmann-Institute,Forschungszentrum Karlsruhe
[2] Institute of Toxicology and Genetics,Cancer Center, Department of Clinical Oncology, Prince of Wales Hospital
[3] The Chinese University of Hong Kong,undefined
来源：
Nature | 2006年 / 442卷
关键词：
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The phosphatase that activates the Merlin tumour suppressor (also known as neurofibromatosis 2) has been identified. It's a myosin phosphatase that is inhibited by the endogenous inhibitor CPI-17, which is often upregulated in human tumours and may contribute to the development of cancer by inactivating Merlin. Taken together, these findings point to a novel cascade of tumour suppressors whose action can be abolished in at least two ways, by mutation (NF2) or upregulation of the putative novel oncogene, CPI-17.
引用
收藏
页码：576 / 579
页数：3
相关论文
共 50 条
  • [1] Tumorigenic transformation by CPI-17 through inhibition of a merlin phosphatase
    Jin, Hongchuan
    Sperka, Tobias
    Herrlich, Peter
    Morrison, Helen
    NATURE, 2006, 442 (7102) : 576 - 579
  • [2] The phosphatase CPI-17 as a regulator of oligodendrocyte degeneration
    Behrangi, N.
    Rennet, M.
    Ostertag, D.
    Kipp, M.
    MULTIPLE SCLEROSIS JOURNAL, 2018, 24 : 845 - 845
  • [3] Inhibition of myosin phosphatase through CPI-17 phosphorylated by Rho-kinase and protein kinase N
    Koyama, M
    Ito, M
    Feng, JH
    Seko, T
    Yamawaki, K
    Isaka, N
    Kaibuchi, K
    Hartshorne, DJ
    Nakano, T
    CIRCULATION, 2000, 102 (18) : 320 - 320
  • [4] The role of CPI-17 in Merlin-dependent small GTPase regulation in oligodendrocytes
    Dornblut, C.
    Morrison, H.
    GLIA, 2015, 63 : E119 - E119
  • [5] Dephosphorylation of CPI-17 by myosin light chain phosphatase (MP)
    Zhao, R
    Mabuchi, K
    Zhang, JH
    Tao, T
    BIOPHYSICAL JOURNAL, 2003, 84 (02) : 102A - 102A
  • [6] Identification of human CPI-17, an inhibitory phosphoprotein for myosin phosphatase
    Yamawaki, K
    Ito, M
    Machida, H
    Moriki, N
    Okamoto, R
    Isaka, N
    Shimpo, H
    Kohda, A
    Okumura, K
    Hartshorne, DJ
    Nakano, T
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 285 (04) : 1040 - 1045
  • [7] CPI-17 and myosin light chain phosphatase expression in smooth muscle
    Woodsome, TP
    Kitazawa, T
    BIOPHYSICAL JOURNAL, 2000, 78 (01) : 111A - 111A
  • [8] In situ CPI-17 kinase and phosphatase in arterial smooth muscle.
    Kitazawa, T
    Eto, M
    Woodsome, TP
    BIOPHYSICAL JOURNAL, 2001, 80 (01) : 393A - 393A
  • [9] Phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by protein kinase N
    Hamaguchi, T
    Ito, M
    Feng, JH
    Seko, T
    Koyama, M
    Machida, H
    Takase, K
    Amano, M
    Kaibuchi, K
    Hartshorne, DJ
    Nakano, T
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 274 (03) : 825 - 830
  • [10] cAMP stabilizes endothelial barrier by activation and assembly of the myosin light chain phosphatase holoenzyme and inhibition of CPI-17
    Aslam, M
    Haertel, FV
    Guenduez, D
    Arshad, M
    Noll, T
    CIRCULATION, 2005, 112 (17) : U196 - U196
12345