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Sci. Signal., 13 March 2012
Vol. 5, Issue 215, p. ra21
Ligand binding to the epidermal growth factor receptor (EGFR) triggers the endocytosis (internalization) of the receptor, which can be degraded or recycled back to the cell surface. Because EGF remains bound, internalized EGFR could continue to signal. Brankatschk et al. investigated how the transcriptional response to EGF was affected by ubiquitination (a posttranslational modification of the EGFR that is required for its endocytic sorting) and endocytosis of cell surface EGFR and by intracellular sorting of internalized EGFR. Whereas interfering with factors that mediate sorting steps of internalized EGFR did not substantially alter the intensity or profile of the EGF-induced transcriptional response, blocking the ubiquitination or endocytosis of the EGFR increased the transcriptional response. The authors suggest that the transcriptional response to activation of the EGFR is rapidly put into motion after receptors at the cell surface are stimulated and before degradative sorting takes place.
Citation: B. Brankatschk, S. P. Wichert, S. D. Johnson, O. Schaad, M. J. Rossner, J. Gruenberg, Regulation of the EGF Transcriptional Response by Endocytic Sorting. Sci. Signal.5, ra21 (2012).
Yonathan Lissanu Deribe, Philipp Wild, Akhila Chandrashaker, Jasna Curak, Mirko H. H. Schmidt, Yannis Kalaidzidis, Natasa Milutinovic, Irina Kratchmarova, Lukas Buerkle, Michael J. Fetchko, Philipp Schmidt, Saranya Kittanakom, Kevin R. Brown, Igor Jurisica, Blagoy Blagoev, Marino Zerial, Igor Stagljar, and Ivan Dikic (22 December 2009) Sci. Signal.2 (102), ra84.
[DOI: 10.1126/scisignal.2000576] |Editor's Summary »|Abstract »|Full Text »|PDF »|Supplementary Materials »