Molecular and Cellular Biochemistry

, Volume 231, Issue 1–2, pp 69–74 | Cite as

Identification of TH1 as an interaction partner of A-Raf kinase

  • Xiang L. Yin
  • She. Chen
  • Jian X. Gu
Article

Abstract

A-Raf is an important intermediate of the growth factor Ras-MAP kinase pathway. In a two-hybrid screen of human fetal liver cDNA library, TH1 was detected as a new interaction partner of A-Raf. TH1 is a highly conserved and widely expressed protein, which was recently cloned by Bonthron DT group. The binding between A-Raf and TH1 was specific, as no binding between TH1 and B-Raf or c-Raf was observed, and the amino-terminal 162 amino acids in the A-Raf regulatory domain were found to be sufficient for this interaction. This specific interaction may have played a critical role in the activation of A-Raf.

A-Raf kinase interaction putative TH1 protein two-hybrid system 

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References

  1. 1.
    Daum G, Eisenmann-Tappe I, Fries HW, Troppmair J, Rapp UR: The ins and outs of Raf kinases. Trends Biochem Sci 19: 474–480, 1994Google Scholar
  2. 2.
    Ghosh S, Xie WQ, Quest AF, Mabrouk GM, Strum JC, Bell RM: The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras. J Biol Chem 269: 10000–10007, 1994Google Scholar
  3. 3.
    Hagemann C, Rapp UR: Isotype-specific functions of Raf kinases. Exp Cell Res 253: 34–46, 1999Google Scholar
  4. 4.
    Heidecker G, Huleihel M, Cleveland JL, Kolch W, Beck TW, Lloyd P, Pawson T, Rapp UR: Mutational activation of c-raf-1 and definition of the minimal transforming sequence. Mol Cell Biol 10: 2503–2512, 1990Google Scholar
  5. 5.
    Storm SM, Cleveland JL, Rapp UR: Expression of raf family protooncogenes in normal mouse tissues. Oncogene 5: 345–351, 1990Google Scholar
  6. 6.
    Sutor, SL, Vroman BT, Armstrong EA, Abraham RT: A phosphatidylinositol 3-kinase-dependent pathway that differentially regulates c-Raf and A-Raf. J Biol Chem 274: 7002–7010, 1999Google Scholar
  7. 7.
    Bogoyevitch MA, Marshall CJ, Sugden PH: Hypertrophic agonists stimulate the activities of the protein kinases c-Raf and A-Raf in cultured ventricular myocytes. J Biol Chem 270: 26303–26310, 1995Google Scholar
  8. 8.
    Boldyreff B, Issinger O: A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit. FEBS Lett 403: 197–199, 1997Google Scholar
  9. 9.
    Hagemann C, Kalmes A, Wixler V, Wixler L, Schuster T, Rapp UR: The regulatory subunit of protein kinase CK2 is a specific A-Raf activator. FEBS Lett 403: 200–202, 1997Google Scholar
  10. 10.
    Beck TW, Huleihel M, Gunnell M, Bonner TI, Rapp UR: The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus. Nucleic Acids Res 15: 595–609, 1987Google Scholar
  11. 11.
    Hoffman CS, Winston F: A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57: 267–272, 1987Google Scholar
  12. 12.
    Appel RD, Bairoch A, Hochstrasser DF: A new generation of information retrieval tools for biologists: The example of the ExPASy WWW server. Trends Biochem Sci 19: 258–260, 1994Google Scholar
  13. 13.
    Vojtek AB, Hollenberg SM, Cooper JA: Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205–214, 1993Google Scholar
  14. 14.
    Wu X, Noh SJ, Zhou G, Dixon JE, Guan K: Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells. J Biol Chem 271: 3265–3271, 1996Google Scholar
  15. 15.
    Michaud NR, Fabian JR, Masthes KD, Morrison DK: 14-3-3 is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3-and Ras-independent manner. Mol Cell Biol 15: 3390–3397, 1995Google Scholar
  16. 16.
    Bonthron DT, Hayward BE, Moran V, Strain L: Characterization of TH1 and CTSZ, two non-imprinted genes downstream of GNAS1 in chromosome 20q13. Hum Genet 107: 165–175, 2000Google Scholar
  17. 17.
    Taniguchi H: Protein myristoylation in protein-lipid and protein-protein interactions. Biophys Chem 13: 129–137, 1999Google Scholar
  18. 18.
    Schaeffer HJ, Catling AD, Eblen ST, Collier LS, Krauss A, Weber MJ:MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 281: 1668–1671, 1998Google Scholar

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Xiang L. Yin
  • She. Chen
  • Jian X. Gu

There are no affiliations available

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