Journal
ONCOGENE
Volume 33, Issue 49, Pages 5619-5625Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2013.504
Keywords
PPAR gamma; MUC1-C; ubiquitin; degradation; ubiquitination; cancer
Funding
- Jiangsu Province Natural Science Foundation [SBK201320232]
- Start Fund of University of JiangSu [12JDG071]
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MUC1-C oncoprotein is associated with colon, breast, ovarian, lung and pancreatic cancers. MUC1-C interacts with intracellular proteins to elicit signaling cascades that induce cell proliferation and tumor growth. Here we report that peroxisome proliferator-activated receptor gamma (PPAR gamma), an E3 ubiquitin ligase, is an inhibitor of MUC1-C-mediated cell proliferation. PPAR gamma does so by binding to and inducing MUC1-C proteasome-dependent degradation that was independent of PPAR gamma transcriptional activity. Lys134 residue was found to be critically important for PPAR gamma-mediated MUC1-C degradation, as it terminated MUC1-C-mediated cell proliferation. These findings demonstrate PPAR gamma induces MUC1-C ubiquitination and degradation that is critical to terminate MUC1-C signaling pathway-elicited cancer.
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