ERK kinase phosphorylates and destabilizes the tumor suppressor FBW7 in pancreatic cancer View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-03-10

AUTHORS

Shunrong Ji, Yi Qin, Si Shi, Xiangyuan Liu, Hongli Hu, Hu Zhou, Jing Gao, Bo Zhang, Wenyan Xu, Jiang Liu, Dingkong Liang, Liang Liu, Chen Liu, Jiang Long, Haijun Zhou, Paul J Chiao, Jin Xu, Quanxing Ni, Daming Gao, Xianjun Yu

ABSTRACT

F-box and WD repeat domain-containing 7 (FBW7) is the substrate recognition component of the Skp1-Cul1-F-box (SCF) ubiquitin ligase complex and functions as a major tumor suppressor by targeting various oncoproteins for degradation. Genomic deletion or mutation of FBW7 has frequently been identified in many human cancers but not in pancreatic ductal adenocarcinoma. Thus it is important to know how the tumor suppressive function of FBW7 is impaired in pancreatic cancer. In this study, we first observed that low FBW7 expression correlated significantly with ERK activation in pancreatic cancer clinical samples, primarily due to KRAS mutations in pancreatic cancer. We further showed that ERK directly interacted with FBW7 and phosphorylated FBW7 at Thr205, which sequentially promoted FBW7 ubiquitination and proteasomal degradation. Furthermore, the phospho-deficient T205A FBW7 mutant is resistant to ERK activation and could significantly suppress pancreatic cancer cell proliferation and tumorigenesis. These results collectively demonstrate how the oncogenic KRAS mutation inhibits the tumor suppressor FBW7, thus revealing an important function of KRAS mutations in promoting pancreatic cancer progression. More... »

PAGES

561-573

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/cr.2015.30

DOI

http://dx.doi.org/10.1038/cr.2015.30

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045676133

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25753158


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