ArticleOncogene2003
Role of TFG sequences outside the coiled-coil domain in TRK-T3 oncogenic activation.
Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Homozygous TFG gene variants expanding the mutational and clinical spectrum of hereditary spastic paraplegia 57 and a review of literature.Journal of human genetics · 2021Article
- Wnt/β-catenin signaling: Structure, assembly and endocytosis of the signalosome.Development, growth & differentiation · 2021Review
- Deep Evolutionary History of the Phox and Bem1 (PB1) Domain Across Eukaryotes.Scientific reports · 2020Article
- Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases.Chemical reviews · 2014Review
- Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators.Frontiers in molecular biosciences · 2014Review
- Immunohistochemical Mapping of TRK-Fused Gene Products in the Rat Brainstem.Acta histochemica et cytochemica · 2012Article
- Expression and Localization of TRK-Fused Gene Products in the Rat Brain and Retina.Acta histochemica et cytochemica · 2012Article
- PB1 domain interaction of p62/sequestosome 1 and MEKK3 regulates NF-kappaB activation.The Journal of biological chemistry · 2010Article
- Intrinsic structural disorder confers cellular viability on oncogenic fusion proteins.PLoS computational biology · 2009Article
- ced-4 and proto-oncogene tfg-1 antagonistically regulate cell size and apoptosis in C. elegans.Current biology : CB · 2008Article
- An in vivo functional genetic screen reveals a role for the TRK-T3 oncogene in tumor progression.Oncogene · 2004Article
- The PB1 domain and the PC motif-containing region are structurally similar protein binding modules.The EMBO journal · 2003Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TRK-T3 oncoprotein, isolated from a human papillary thyroid tumor, arises from the fusion between the N-terminal domain of the TFG gene and the tyrosine kinase domain of the NTRK1 receptor. The 68 kDa TRK-T3 oncoprotein displays a constitutive tyrosine kinase activity resulting in its capability to transform NIH3T3 cells. The TFG portion of TRK-T3 contains a coiled-coil domain, which mediates protein oligomerization essential for the oncogene constitutive activation, and several consensus sites for protein interaction. In this study, we investigate the role of TFG sequences outside the coiled-coil domain on TRK-T3 activation, We constructed four mutants carrying different deletions of TFG sequences and expressed them in mammalian cells. By performing biochemical and biological assays we demonstrated that all the deleted regions are required for TRK-T3 activation, as they are involved in different mechanisms such as protein processing, formation of stable and/or functional complexes, and possible interaction with other proteins. By constructing site-specific mutants, we demonstrated a crucial role for a PB1 domain and a considerable contribution of an SH2-binding motif in TRK-T3 oncogenic activation. This work establishes an important role for TFG sequences outside the coiled-coil domain in the activation of the thyroid TRK-T3 oncogene.
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