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

doi:10.18632/oncotarget.2510

Oncotarget

Oncotarget (a primarily oncology-focused, peer-reviewed, open access journal) aims to maximize research impact through insightful peer-review; eliminate borders between specialties by linking different fields of oncology, cancer research and biomedical sciences; and foster application of basic and clinical science.

Its scope is unique. The term "oncotarget" encompasses all molecules, pathways, cellular functions, cell types, and even tissues that can be viewed as targets relevant to cancer as well as other diseases. The term was introduced in the inaugural Editorial, Introducing Oncotarget.

As of January 1, 2022, Oncotarget has shifted to a continuous publishing model. Papers will now be published continuously within yearly volumes in their final and complete form and then quickly released to Pubmed.

Subscribe to receive alerts once a paper has been published by Oncotarget.

Impact Journals, LLC is the publisher of Oncotarget: www.impactjournals.com.

Impact Journals is a member of the Wellcome Trust List of Compliant Publishers.

Impact Journals is a member of the Society for Scholarly Publishing.

On December 23, 2022, Oncotarget server experienced a DDoS attack. As a result, Oncotarget site was inaccessible for a few hours. Oncotarget team swiftly dealt with the situation and took it under control. This malicious action will be reported to the FBI.

Research Papers:

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 and Jen-Liang Su _

PDF | HTML | Supplementary Files | How to cite

Oncotarget. 2014; 5:10558-10570. https://doi.org/10.18632/oncotarget.2510

Metrics: PDF 3105 views | HTML 3873 views | ?

Abstract

Yi-Wen Chang1,*, Hsin-An Chen2,3,*, Chi-Feng Tseng1,4, Chih-Chen Hong1, Jui-Ti Ma1,4, Mien-Chie Hung5,6,7,8, Chih-Hsiung Wu2,3, Ming-Te Huang2,3 and Jen-Liang Su1,5,6,7

1 National Institute of Cancer Research, National Health Research Institutes, Zhunan, Miaoli Country, Taiwan

2 Graduate Institute of Clinical Medicine, College of Medicine, Taipei Medical University, Taipei, Taiwan

3 Division of General Surgery, Department of Surgery, Shuang Ho Hospital, Taipei Medical University, New Taipei City, Taiwan

4 Graduate Program of Biotechnology in Medicine College of Life Science, National Tsing Hua University, Hsinchu, Taiwan

5 Graduate Institute of Cancer Biology, China Medical University, Taichung, Taiwan

6 Center for Molecular Medicine, China Medical University Hospital, Taichung, Taiwan

7 Department of Biotechnology, Asia University, Taichung, Taiwan

8 Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas, USA

* These authors contributed equally to this work

Correspondence:

Jen-Liang Su , email:

Keywords: acetylation, adenovirus type 5 E1A, HSPA5/GRP78/Bip, metastasis, ubiquitination

Received: July 02, 2014 Accepted: September 24, 2014 Published: September 25, 2014

Abstract

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.

All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 4.0 License.
PII: 2510

Publication Alerts

Research Papers:

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

Abstract