Cited by 270

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TGF-β-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI

Chaudhury, Arindam, Hussey, George S., Ray, Partho S, Jin, Ge, Fox, Paul L., Howe, Philip H.·2010·Nature Cell Biology

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Crossref · 10.1038/ncb2029

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  • Several mechanisms have been suggested for Dab2 involvement in the TGF-beta pathway, but their actual operation in intact animals and physiological settings has yet to be demonstrated.

    “Thus, several mechanisms have been suggested for the involvement of Dab2 in TGF-beta pathway, such as receptor recycling, adapting function for Smad activation, or non-canonical TGF-beta signaling through the Ras-MAPK pathway, although the actual operation of these mechanisms in intact animals and physiological settings have yet to be demonstrated.”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Chaudhury et al., 2010

    The paper’s Abstract describes Dab2 as a mediator of TGF-β-induced EMT and says its precise function downstream of hnRNP E1 is difficult to define. It does not identify receptor recycling, Smad activation, or Ras–MAPK signaling as proposed Dab2 mechanisms, nor does it specifically say that those mechanisms remain untested in intact animals or physiological settings. No page number is available in our copy. (LLM, conf=0.79)

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Research works printed but not linked: 33

  1. Massagué, J. TGFβ in cancer. Cell 134, 215–230 (2008). · DOI · Paper page
  2. Bierie, B. & Moses, H. L. TGF-β and cancer. Cytokine Growth Factor Rev. 17, 29–40 (2006). · DOI
  3. Zavadil, J. & Bottinger, E. P. TGF-β and epithelial-to-mesenchymal transitions. Oncogene 24, 5764–5774 (2005). · DOI
  4. Thiery, J. P. & Sleeman, J. P. Complex networks orchestrate epithelial–mesenchymal transitions. Nature Rev. Mol. Cell. Biol. 7, 131–142 (2006). · DOI
  5. Miettinen, P. J., Ebner, R., Lopez, A. R. & Derynck, R. TGF-β induced transdifferentiation of mammary epithelial cells to mesenchymal cells: involvement of type I receptors. J. Cell Biol. 127, 2021–2036 (1994). · DOI
  6. Thuault, S. et al. Transforming growth factor-β employs HMGA2 to elicit epithelial–mesenchymal transition. J. Cell Biol. 174, 175–183 (2006). · DOI
  7. Oft, M. et al. TGF-β1 and Ha-Ras collaborate in modulating the phenotypic plasticity and invasiveness of epithelial tumor cells. Genes Dev. 10, 2462–2477 (1996). · DOI
  8. Prunier, C. & Howe, P. H. Disabled-2 (Dab2) is required for transforming growth factor β-induced epithelial to mesenchymal transition (EMT). J. Biol. Chem. 280, 17540–17548 (2005). · DOI · Paper page
  9. Waerner, T. et al. ILEI: a cytokine essential for EMT, tumor formation, and late events in metastasis in epithelial cells. Cancer Cell 10, 227–239 (2006). · DOI
  10. Greinwald, J. H. Jr et al. Localization of a novel gene for nonsyndromic hearing loss (DFNB17) to chromosome region 7q31. Am. J. Med. Genet. 78, 107–113 (1998). · DOI
  11. Zhu, Y. et al. Cloning, expression, and initial characterization of a novel cytokine-like gene family. Genomics 80, 144–150 (2002). · DOI
  12. Pradet-Balade, B., Boulme, F., Beug, H., Mullner, E. W. & Garcia-Sanz, J. A. Translation control: bridging the gap between genomics and proteomics? Trends Biochem. Sci. 26, 225–229 (2001). · DOI
  13. Kang, Y. & Massagué, J. Epithelial–mesenchymal transitions: twist in development and metastasis. Cell 118, 277–279 (2004). · DOI
  14. Grillo, G., Licciulli, F., Liuni, S., Sbisa, E. & Pesole, G. PatSearch: a program for the detection of patterns and structural motifs in nucleotide sequences. Nucleic Acids Res. 31, 3608–3612 (2003). · DOI
  15. Ostareck, D. H. et al. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89, 597–606 (1997). · DOI
  16. Bakin, A. V., Tomlinson, A. K., Bhowmick, N. A., Moses, H. L. & Arteaga, C. L. Phosphatidylinositol 3-kinase function is required for transforming growth factor β-mediated epithelial to mesenchymal transition and cell migration. J. Biol. Chem. 275, 36803–36810 (2000). · DOI
  17. Kattla, J. J., Carew, R. M., Heljic, M., Godson, C. & Brazil, D. P. Protein kinase B/Akt activity is involved in renal TGF-β1-driven epithelial–mesenchymal transition in vitro and in vivo. Am. J. Physiol. Renal Physiol. 295, F215–F225 (2008). · DOI
  18. Kato, M. et al. TGF-β activates Akt kinase through a microRNA-dependent amplifying circuit targeting PTEN. Nature Cell Biol. 11, 881–889 (2009). · DOI
  19. Meng, Q. et al. Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1. Proc. Natl Acad. Sci. USA 104, 5866–5871 (2007). · DOI
  20. Brazil, D. P. & Hemmings, B. A. Ten years of protein kinase B signaling: a hard Akt to follow. Trends Biochem. Sci. 26, 657–664 (2001). · DOI · Paper page
  21. Kato, S., Ding, J. & Du, K. Differential activation of CREB by Akt1 and Akt2. Biochem. Biophys. Res. Commun. 354, 1061–1066 (2007). · DOI
  22. Lamouille, S. & Derynck, R. Cell size and invasion in TGF-β-induced epithelial to mesenchymal transition is regulated by activation of the mTOR pathway. J. Cell Biol. 178, 437–451 (2007). · DOI
  23. Irie, H. Y. et al. Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial–mesenchymal transition. J. Cell Biol. 171, 1023–1034 (2005). · DOI
  24. Keene, J. D. & Tenenbaum, S. A. Eukaryotic mRNPs may represent posttranscriptional operons. Mol. Cell 9, 1161–1167 (2002). · DOI
  25. Nishinakamura, H. et al. An RNA-binding protein αCP-1 is involved in the STAT3-mediated suppression of NF-κB transcriptional activity. Int. Immunol. 19, 609–619 (2007). · DOI
  26. Wildey, G. M., Patil, S. & Howe, P. H. Smad3 potentiates transforming growth factor-β (TGF-β)-induced apoptosis and expression of the BH3-only protein Bim in WEHI 231 B lymphocytes J. Biol. Chem. 278, 18069–18077 (2003). · DOI
  27. Hocevar, B. A., Brown, T. L. & Howe, P. H. TGF-β induces fibronectin synthesis through a c-Jun N-terminal kinase-dependent, Smad4-independent pathway. EMBO J. 18, 1345–1356 (1999). · DOI
  28. Mazumder, B. & Fox, P. L. Delayed translational silencing of ceruloplasmin transcript in γ interferon-activated U937 monocytic cells: role of the 3′ untranslated region. Mol. Cell. Biol. 19, 6898–6905 (1999). · DOI
  29. Hampton, M. B., Zhivotovsky, B., Slater, A. F., Burgess, D. H. & Orrenius, S. Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts. Biochem. J. 329, 95–99 (1998). · DOI
  30. Ray, P. S. & Fox, P. L. A post-transcriptional pathway represses monocyte VEGF-A expression and angiogenic activity. EMBO J. 26, 3360–3372 (2007). · DOI
  31. Legagneux, V., Bouvet, P., Omilli, F., Chevalier, S. & Osborne, H. B. Identification of RNA-binding proteins specific to Xenopus Eg maternal mRNAs: association with the portion of Eg2 mRNA that promotes deadenylation in embryos. Development 116, 1193–1202 (1992). · DOI
  32. Sampath, P. et al. Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Cell 119, 195–208 (2004). · DOI · Paper page
  33. Qi, X. J., Wildey, G. M. & Howe, P. H. Evidence that Ser87 of BimEL is phosphorylated by Akt and regulates BimEL apoptotic function. J. Biol. Chem. 281, 813–823 (2006). · DOI

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Metadata

Authors
Chaudhury, A., Hussey, G. S., Ray, P. S., Jin, G., Fox, P. L., & Howe, P. H.
Venue
Nature Cell Biology
Published
2010-02-14
Volume
12
Issue
3
Pages
286-293
ISSN
  • 1465-7392
  • 1476-4679
Cited by
270
References
3
Language
en

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