Abstract
Abstract Neddylation plays a distinct role in stabilization of a subset of ribosomal proteins. How ribosomal proteins are neddylated and whether their neddylation plays any biological roles in cell growth and survival remains elusive. Here we report that ribosomal protein S27-like (RPS27L) and its family member RPS27 is subjected to neddylation by MDM2 E3 ubiquitin ligase, and deneddylation by NEDP1. Disrupting neddylation with MLN4924, a newly discovered small molecule inhibitor of neddylation pathway, destabilized RPS27L and RPS27. Moreover, silencing of RPS27L and RPS27 sensitized breast cancer cells to MLN4924-induced apoptosis. Our results suggest that neddylation stabilizes RPS27L and RPS27, and confers the survival of breast cancer cells. Citation Format: Yongchao Zhao, Xiufang Xiong, Yi Sun. Neddylation of ribosomal protein S27-like and RPS27 regulates survival of breast cancer cells. [abstract]. In: Proceedings of the 105th Annual Meeting of the American Association for Cancer Research; 2014 Apr 5-9; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2014;74(19 Suppl):Abstract nr 4436. doi:10.1158/1538-7445.AM2014-4436
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