Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2012-10

AUTHORS

Fresia Pareja, Daniela Aleida Ferraro, Chanan Rubin, Hadas Cohen-Dvashi, Fan Zhang, Sebastian Aulmann, Nir Ben-Chetrit, Gur Pines, Roy Navon, Nicola Crosetto, Wolfgang Köstler, Silvia Carvalho, Sara Lavi, Fernando Schmitt, Ivan Dikic, Zohar Yakhini, Peter Sinn, Gordon B. Mills, Yosef Yarden

ABSTRACT

Once stimulated, the epidermal growth factor receptor (EGFR) undergoes self-phosphorylation, which, on the one hand, instigates signaling cascades, and on the other hand, recruits CBL ubiquitin ligases, which mark EGFRs for degradation. Using RNA interference screens, we identified a deubiquitinating enzyme, Cezanne-1, that opposes receptor degradation and enhances EGFR signaling. These functions require the catalytic- and ubiquitin-binding domains of Cezanne-1, and they involve physical interactions and transphosphorylation of Cezanne-1 by EGFR. In line with the ability of Cezanne-1 to augment EGF-induced growth and migration signals, the enzyme is overexpressed in breast cancer. Congruently, the corresponding gene is amplified in approximately one third of mammary tumors, and high transcript levels predict an aggressive disease course. In conclusion, deubiquitination by Cezanne-1 curtails degradation of growth factor receptors, thereby promotes oncogenic growth signals. More... »

PAGES

4599

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/onc.2011.587

    DOI

    http://dx.doi.org/10.1038/onc.2011.587

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1034726500

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/22179831


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