ERK promotes tumorigenesis by inhibiting FOXO3a via MDM2-mediated degradation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2008-02

AUTHORS

Jer-Yen Yang, Cong S. Zong, Weiya Xia, Hirohito Yamaguchi, Qingqing Ding, Xiaoming Xie, Jing-Yu Lang, Chien-Chen Lai, Chun-Ju Chang, Wei-Chien Huang, Hsin Huang, Hsu-Ping Kuo, Dung-Fang Lee, Long-Yuan Li, Huang-Chun Lien, Xiaoyun Cheng, King-Jen Chang, Chwan-Deng Hsiao, Fuu-Jen Tsai, Chang-Hai Tsai, Aysegul A. Sahin, William J. Muller, Gordon B. Mills, Dihua Yu, Gabriel N. Hortobagyi, Mien-Chie Hung

ABSTRACT

The RAS-ERK pathway is known to play a pivotal role in differentiation, proliferation and tumour progression. Here, we show that Erk downregulates Forkhead box O 3a (FOXO3a) by directly interacting with and phosphorylating FOXO3a at Ser 294, Ser 344 and Ser 425, which consequently promotes cell proliferation and tumorigenesis. The ERK-phosphorylated FOXO3a degrades via an MDM2-mediated ubiquitin-proteasome pathway. However, the non-phosphorylated FOXO3a mutant is resistant to the interaction and degradation by murine double minute 2 (MDM2), thereby resulting in a strong inhibition of cell proliferation and tumorigenicity. Taken together, our study elucidates a novel pathway in cell growth and tumorigenesis through negative regulation of FOXO3a by RAS-ERK and MDM2. More... »

PAGES

138-148

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncb1676

DOI

http://dx.doi.org/10.1038/ncb1676

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029052135

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/18204439


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