Journal
ONCOTARGET
Volume 5, Issue 21, Pages 10558-10570Publisher
IMPACT JOURNALS LLC
DOI: 10.18632/oncotarget.2510
Keywords
acetylation; adenovirus type 5 E1A; HSPA5/GRP78/Bip; metastasis; ubiquitination
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Funding
- National Science Council grant from Taiwan [NSC 101-2320-B-400-016-MY3, NSC 102-2314-B-038-028-MY3, NSC 103-2314-B-038-059]
- National Health Research Institutes grant from Taiwan [CA-102-PP-41]
- Taipei Medical University-Shuang Ho Hospital, Ministry of Health and Welfare grant from Taiwan [103TMU-SHH-26]
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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.
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