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Tpl-2 Is an Oncogenic Kinase That Is Activated By Carboxy-Terminal Truncation

  1. Author:
    Ceci, J. D.
    Patriotis, C. P.
    Tsatsanis, C.
    Makris, A. M.
    Kovatch, R.
    Swing, D. A.
    Jenkins, N. A.
    Tsichlis, P. N.
    Copeland, N. G.

  2. Author Address

    Copeland NG NCI FREDERICK CANC RES FACIL FREDERICK, MD 21702 USA NCI FREDERICK CANC RES FACIL FREDERICK, MD 21702 USA NCI DEV CTR FREDERICK, MD 21702 USA FOX CHASE CANC CTR PHILADELPHIA, PA 19111 USA PATHOL ASSOCIATES INC FREDERICK, MD 21702 USA
    1. Year: 1997
  2. Journal: Genes & Development
    1. 11
    2. 6
    3. Pages: 688-700
  4. Type of Article: Article
  1. Abstract:

    Provirus insertion in the last intron of the Tpl-2 gene in retrovirus-induced rat T-cell lymphomas results in the enhanced expression of a carboxy-terminally truncated Tpl-2 kinase. Here we show that the truncated protein exhibits an approximately sevenfold higher catalytic activity and is two- to threefold more efficient in activating the MAPK and SAPK pathways relative to the wild-type protein. The truncated Tpl-2 protein and a GST fusion of the Tpl-2 carboxy-terminal tail interact when coexpressed in Sf9 cells. Their interaction down-regulates the kinase activity of the truncated protein suggesting that tail-directed intramolecular interactions regulate the Tpl-2 kinase. Tpl-2 transgenic mice expressing the wild-type protein from the proximal Lck promoter fail to show a biological phenotype, whereas mice expressing the truncated protein develop large-cell lymphoblastic lymphomas of T-cell origin. These results show that Tpl-2 is an oncogenic kinase that is activated by carboxy-terminal truncation. [References: 46]

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