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TGF‐β activates Erk MAP kinase signalling through direct phosphorylation of ShcA
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Dab2 modulates the non-canonical pathways of TGF-beta by suppressing Ras/MAPK activation.
“Therefore, it was concluded that Dab2 modulates the non-canonical pathways of TGF-beta by suppressing Ras/MAPK activation”
From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Lee et al., 2007
The Introduction and the section ‘Direct induction of MAP kinase by TGF-b is mediated by ShcA’ describe TGF-β-induced Ras/MAPK signaling and its attenuation by ShcA mutants. The passages provided and searches for Dab2 and Disabled-2 yielded no discussion of whether Dab2 suppresses that pathway, which is the claim attributed to this source. (LLM, conf=0.73)
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TGF-β Signaling in Tumor Suppression and Cancer Progression
Derynck, R., Akhurst, R. J., & Balmain, A. (2001) · Nature Genetics · doi:10.1038/ng1001-117 · Cited by 2,275
Self-citationThe p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712
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Research works printed but not linked: 43
- Attisano L, Wrana JL (2002) Signal transduction by the TGF‐β superfamily. Science 296: 1646–1647 · DOI
- Berrou E, Fontenay‐Roupie M, Quarck R, McKenzie FR, Lévy‐Toldano S, Tobelem G, Bryckaert M (1996) Transforming growth factor β1 inhibits mitogen‐activated protein kinase induced by basic fibroblast growth factor in smooth muscle cells. Biochem J 316: 167–173 · DOI
- Cano E, Hazzalin CA, Kardalinou E, Buckle RS, Mahadevan LC (1995) Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG‐14 phosphorylation or c‐fos and c‐jun induction. J Cell Sci 108: 3599–3609 · DOI
- Chen RH, Moses HL, Maruoka EM, Derynck R, Kawabata M (1995) Phosphorylation‐dependent interaction of the cytoplasmic domains of the type I and type II transforming growth factor‐β receptors. J Biol Chem 270: 12235–12241 · DOI
- Cooper JA, Sefton BM, Hunter T (1983) Detection and quantification of phosphotyrosine in proteins. Methods Enzymol 99: 387–402 · DOI
- Davies M, Robinson M, Smith E, Huntley S, Prime S, Paterson I (2005) Induction of an epithelial to mesenchymal transition in human immortal and malignant keratinocytes by TGF‐β1 involves MAPK, Smad and AP‐1 signalling pathways. J Cell Biochem 95: 918–931 · DOI
- Derynck R, Zhang YE (2003) Smad‐dependent and Smad‐independent pathways in TGF‐β family signalling. Nature 425: 577–584 · DOI
- Feng XH, Derynck R (1996) Ligand‐independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF‐β receptors. J Biol Chem 271: 13123–13129 · DOI
- Feng XH, Filvaroff EH, Derynck R (1995) Transforming growth factor‐β (TGF‐β)‐induced down‐regulation of cyclin A expression requires a functional TGF‐β receptor complex. Characterization of chimeric and truncated type I and type II receptors. J Biol Chem 270: 24237–24245 · DOI
- Frippiat C, Chen QM, Zdanov S, Magalhäes JP, Remacle J, Toussaint O (2001) Subcytotoxic H2O2 stress triggers a release of transforming growth factor‐β1, which induces biomarkers of cellular senescence of human diploid fibroblasts. J Biol Chem 276: 2531–2537 · DOI
- Gotoh N, Muroya K, Hattori S, Nakamura S, Chida K, Shibuya M (1995) The SH2 domain of Shc suppresses EGF‐induced mitogenesis in a dominant negative manner. Oncogene 11: 2525–2533
- Gotoh N, Tojo A, Shibuya M (1996) A novel pathway from phosphorylation of tyrosine residues 239/240 of Shc, contributing to suppress apoptosis by IL‐3. EMBO J 15: 6197–6204 · DOI
- Hanks SK, Hunter T (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9: 576–596 · DOI
- Huse M, Chen YG, Massagué J, Kuriyan J (1999) Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12. Cell 96: 425–436 · DOI
- Inman GJ, Nicolas FJ, Callahan JF, Harling JD, Gaster LM, Reith AD, Laping NJ, Hill CS (2002) SB‐431542 is a potent and specific inhibitor of transforming growth factor‐β superfamily type I activin receptor‐like kinase (ALK) receptors ALK4, ALK5, and ALK7. Mol Pharmacol 62: 65–74 · DOI
- Kavanaugh WM, Williams LT (1994) An alternative to SH2 domains for binding tyrosine‐phosphorylated proteins. Science 266: 1862–1865 · DOI
- Kisielow M, Kleiner S, Nagasawa M, Faisal A, Nagamine Y (2002) Isoform‐specific knockdown and expression of adaptor protein ShcA using small interfering RNA. Biochem J 363: 1–5 · DOI
- Kretzschmar M, Doody J, Timokhina I, Massagué J (1999) A mechanism of repression of TGFβ/Smad signaling by oncogenic Ras. Genes Dev 13: 804–816 · DOI
- Lai KM, Pawson T (2000) The ShcA phosphotyrosine docking protein sensitizes cardiovascular signaling in the mouse embryo. Genes Dev 14: 1132–1145 · DOI
- Lawler S, Feng XH, Chen RH, Maruoka EM, Turck CW, Griswold‐Prenner I, Derynck R (1997) The type II transforming growth factor‐β receptor autophosphorylates not only on serine and threonine but also on tyrosine residues. J Biol Chem 272: 14850–14859 · DOI
- Lee MK, Zhao J, Smith S, Tefft JD, Bringas Jr P, Hwang C, Warburton D (1998) The Shc 66 and 46 kDa isoforms are differentially downregulated at parturition in the fetal mouse lung. Pediatr Res 44: 850–859 · DOI
- Lindberg RA, Quinn AM, Hunter T (1992) Dual‐specificity protein kinases: will any hydroxyl do? Trends Biochem Sci 17: 114–119 · DOI
- Lotti LV, Lanfrancone L, Migliaccio E, Zompetta C, Pelicci G, Salcini AE, Falini B, Pelicci PG, Torrisi MR (1996) Shc proteins are localized on endoplasmic reticulum membranes and are redistributed after tyrosine kinase receptor activation. Mol Cell Biol 16: 1946–1954 · DOI
- Luzi L, Confalonieri S, di Fiore PP, Pelicci PG (2000) Evolution of Shc functions from nematode to human. Curr Opin Genet Dev 10: 668–674 · DOI
- Lyons RM, Miller DA, Graycar JL, Moses HL, Derynck R (1991) Differential binding of transforming growth factor‐β1, ‐β2, and ‐β3 by fibroblasts and epithelial cells measured by affinity cross‐linking of cell surface receptors. Mol Endocrinol 5: 1887–1896 · DOI
- Macias‐Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL (1996) MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87: 1215–1224 · DOI
- Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S (2002) The protein kinase complement of the human genome. Science 298: 1912–1934 · DOI · Paper page
- Massagué J (2000) How cells read TGF‐β signals. Nat Rev Mol Cell Biol 1: 169–178 · DOI
- Migliaccio E, Mele S, Salcini AE, Pelicci G, Lai KM, Superti Furga G, Pawson T, di Fiore PP, Lanfrancone L, Pelicci PG (1997) Opposite effects of the p52Shc/p46Shc and p66Shc splicing isoforms on the EGF receptor‐MAP kinase‐fos signalling pathway. EMBO J 16: 706–716 · DOI
- Mucsi I, Skorecki KL, Goldberg HJ (1996) Extracellular signal‐regulated kinase and the small GTP‐binding protein, Rac, contribute to the effects of transforming growth factor‐β1 on gene expression. J Biol Chem 271: 16567–16572 · DOI
- Mulder KM (2000) Role of Ras and Mapks in TGFβ signaling. Cytokine Growth Factor Rev 11: 23–35 · DOI · Paper page
- Olsson N, Piek E, Sundstrom M, ten Dijke P, Nilsson G (2001) Transforming growth factor‐β‐mediated mast cell migration depends on mitogen‐activated protein kinase activity. Cell Signal 13: 483–490 · DOI
- Pelicci G, Lanfrancone L, Grignani F, McGlade J, Cavallo F, Forni G, Nicoletti I, Pawson T, Pelicci PG (1992) A novel transforming protein (Shc) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70: 93–104 · DOI
- Qi M, Elion EA (2005) MAP kinase pathways. J Cell Sci 118: 3569–3572 · DOI
- Ravichandran KS (2001) Signaling via Shc family adapter proteins. Oncogene 20: 6322–6330 · DOI
- Simeone DM, Zhang L, Graziano K, Nicke B, Pham T, Schaefer C, Logsdon CD (2001) Smad4 mediates activation of mitogen‐activated protein kinases by TGF‐β in pancreatic acinar cells. Am J Physiol Cell Physiol 281: C311–C319 · DOI
- Thomas D, Bradshaw RA (1997) Differential utilization of ShcA tyrosine residues and functional domains in the transduction of epidermal growth factor‐induced mitogen‐activated protein kinase activation in 293T cells and nerve growth factor‐induced neurite outgrowth in PC12 cells. Identification of a new Grb2‐2‐Sos1 binding site. J Biol Chem 272: 22293–22299 · DOI
- Trub T, Choi WE, Wolf G, Ottinger E, Chen Y, Weiss M, Shoelson SE (1995) Specificity of the PTB domain of Shc for β turn‐forming pentapeptide motifs amino‐terminal to phosphotyrosine. J Biol Chem 270: 18205–18208 · DOI
- van der Geer P, Wiley S, Gish GD, Pawson T (1996) The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein‐protein interactions. Curr Biol 6: 1435–1444 · DOI
- Ventura A, Maccarana M, Raker VA, Pelicci PG (2004) A cryptic targeting signal induces isoform‐specific localization of p46Shc to mitochondria. J Biol Chem 279: 2299–2306 · DOI
- Wrana JL, Attisano L, Carcamo J, Zentella A, Doody J, Laiho M, Wang XF, Massagué J (1992) TGFβ signals through a heteromeric protein kinase receptor complex. Cell 71: 1003–1014 · DOI
- Yamashita H, ten Dijke P, Franzen P, Miyazono K, Heldin CH (1994) Formation of hetero‐oligomeric complexes of type I and type II receptors for transforming growth factor‐β. J Biol Chem 269: 20172–20178 · DOI
- Yasuda K, Aoshiba K, Nagai A (2003) Transforming growth factor‐β promotes fibroblast apoptosis induced by H2O2. Exp Lung Res 29: 123–134 · DOI
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Metadata
- Authors
- Lee, M. K., Pardoux, C., Hall, M. C., Lee, P. S., Warburton, D., Qing, J., Smith, S. M., & Derynck, R.
- Venue
- The EMBO Journal
- Published
- 2007-08-02
- Volume
- 26
- Issue
- 17
- Pages
- 3957-3967
- ISSN
- 0261-4189
- 1460-2075
- Cited by
- 527
- References
- 2
- Language
- en
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