De-acetylation and degradation of HSPA5 is critical for E1A metastasis suppression in breast cancer cells

Yi Wen Chang, Hsin An Chen, Chi Feng Tseng, Chih Chen Hong, Jui Ti Ma, Mien Chie Hung, Chih Hsiung Wu, Ming Te Huang, Jen Liang Su

研究成果: 雜誌貢獻文章同行評審

19 引文 斯高帕斯(Scopus)

摘要

Elevated expression of heat shock protein 5 (HSPA5) promotes drug resistance and metastasis and is a marker of poor prognosis in breast cancer patients. Adenovirus type 5 E1A gene therapy has demonstrated antitumor efficacy but the mechanisms of metastasis-inhibition are unclear. Here, we report that E1A interacts with p300 histone acetyltransferase (HAT) and blocks p300-mediated HSPA5 acetylation at K353, which in turn promotes HSPA5 ubiquitination by GP78 (E3 ubiquitin ligase) and subsequent proteasome-mediated degradation. Our findings point out the Ying-Yang regulation of two different post-translational modifications (ubiquitination and acetylation) of HSPA5 in tumor metastasis.

原文英語
頁(從 - 到)10558-10570
頁數13
期刊Oncotarget
5
發行號21
DOIs
出版狀態已發佈 - 2014

ASJC Scopus subject areas

  • 腫瘤科

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