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Gene Review

Tpr  -  translocated promoter region, nuclear...

Rattus norvegicus

Synonyms: Megator, NPC-associated intranuclear protein, Nucleoprotein TPR, Translocated promoter region protein
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High impact information on Tpr

  • Injection of anti-Tpr antibodies into mitotic cells resulted in depletion of Tpr from the nuclear envelope without loss of other pore complex basket proteins [1].
  • Thus, Nup153 and Tpr are major physiological binding sites for importin beta [2].
  • Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr [2].
  • Surprisingly, the Grb2 mutants blocked activation of the JNK/SAPK but not MAP kinase activity induced by the Tpr-Met oncoprotein [3].
  • This indicates that reassembly of the NPC after mitosis is a stepwise process, and that the Tpr-containing peripheral structures are assembled later than p62 [4].

Biological context of Tpr

  • These data indicate that the presence of the juxtamembrane domain counterbalances the Tpr-Met transforming potential and therefore the loss of the exon encoding the juxtamembrane domain is crucial in the generation of the active TPR-MET oncogene [5].
  • To examine the role of RTK activated signal transduction pathways to processes involved in cell transformation, we have exploited the oncogenic derivative of the Met RTK (Tpr-Met) [6].
  • In order to determine the sites of tyrosine phosphorylation in the Tpr-Met oncoprotein, in vitro mutagenesis, phosphopeptide mapping, and dephosphorylation protection assays were performed [7].
  • We have identified two tyrosine residues within the catalytic domain of the Tpr-Met oncoprotein (Y365, Y366) and Met receptor (Y1234, Y1235) that are phosphorylated and essential for both the catalytic and biological activity of the oncoprotein and receptor [7].
  • Variables monitored were colonic (Tc) and tail skin (Tsk) temperatures (experiment 1); BP (experiment 2); hypothalamic temperature (Thy), M (from oxygen consumption), and Tsk (experiment 3); and preferred Ta (Tpr) and abdominal temperature (experiment 4) [8].

Anatomical context of Tpr

  • Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex [4].
  • These data are consistent with a single tyrosine residue in the Tpr-Met oncoprotein being essential for the activation of several signalling pathways which lead to the transformation of Fr3T3 fibroblasts [9].

Associations of Tpr with chemical compounds

  • Tpr-Met is a member of a family of tyrosine kinase oncoproteins generated following genomic rearrangement and has constitutive kinase activity [10].

Other interactions of Tpr

  • As a consequence of this rearrangement the Tpr-Met fusion oncoprotein is localized to the cytoplasm and is a constitutively activated kinase [9].

Analytical, diagnostic and therapeutic context of Tpr

  • The enzymatic behavior of Tpr-Met and Tpr-juxtaMet was the same, while Tpr-juxtaMet ability to associate cytoplasmic signal transducers and to elicit downstream signaling was severely impaired [5].


  1. Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. Frosst, P., Guan, T., Subauste, C., Hahn, K., Gerace, L. J. Cell Biol. (2002) [Pubmed]
  2. Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. Shah, S., Tugendreich, S., Forbes, D. J. Cell Biol. (1998) [Pubmed]
  3. Activation of the JNK pathway is essential for transformation by the Met oncogene. Rodrigues, G.A., Park, M., Schlessinger, J. EMBO J. (1997) [Pubmed]
  4. Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. Byrd, D.A., Sweet, D.J., Panté, N., Konstantinov, K.N., Guan, T., Saphire, A.C., Mitchell, P.J., Cooper, C.S., Aebi, U., Gerace, L. J. Cell Biol. (1994) [Pubmed]
  5. Loss of the exon encoding the juxtamembrane domain is essential for the oncogenic activation of TPR-MET. Vigna, E., Gramaglia, D., Longati, P., Bardelli, A., Comoglio, P.M. Oncogene (1999) [Pubmed]
  6. Use of signal specific receptor tyrosine kinase oncoproteins reveals that pathways downstream from Grb2 or Shc are sufficient for cell transformation and metastasis. Saucier, C., Papavasiliou, V., Palazzo, A., Naujokas, M.A., Kremer, R., Park, M. Oncogene (2002) [Pubmed]
  7. Identification of tyrosine 489 in the carboxy terminus of the Tpr-Met oncoprotein as a major site of autophosphorylation. Kamikura, D.M., Naujokas, M.A., Park, M. Biochemistry (1996) [Pubmed]
  8. Endotoxin shock: thermoregulatory mechanisms. Romanovsky, A.A., Shido, O., Sakurada, S., Sugimoto, N., Nagasaka, T. Am. J. Physiol. (1996) [Pubmed]
  9. Efficient cell transformation by the Tpr-Met oncoprotein is dependent upon tyrosine 489 in the carboxy-terminus. Fixman, E.D., Naujokas, M.A., Rodrigues, G.A., Moran, M.F., Park, M. Oncogene (1995) [Pubmed]
  10. Efficient cellular transformation by the Met oncoprotein requires a functional Grb2 binding site and correlates with phosphorylation of the Grb2-associated proteins, Cbl and Gab1. Fixman, E.D., Holgado-Madruga, M., Nguyen, L., Kamikura, D.M., Fournier, T.M., Wong, A.J., Park, M. J. Biol. Chem. (1997) [Pubmed]
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