The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1.
dc.contributor.author | Huang, Nai-Jia | |
dc.contributor.author | Zhang, Liguo | |
dc.contributor.author | Tang, Wanli | |
dc.contributor.author | Chen, Chen | |
dc.contributor.author | Yang, Chih-Sheng | |
dc.contributor.author | Kornbluth, Sally | |
dc.coverage.spatial | United States | |
dc.date.accessioned | 2014-03-06T16:00:39Z | |
dc.date.issued | 2012-04-30 | |
dc.description.abstract | Proapoptotic Bcl-2 family members, such as Bax, promote release of cytochrome c from mitochondria, leading to caspase activation and cell death. It was previously reported that modulator of apoptosis protein 1 (MOAP-1), an enhancer of Bax activation induced by DNA damage, is stabilized by Trim39, a protein of unknown function. In this paper, we show that MOAP-1 is a novel substrate of the anaphase-promoting complex (APC/C(Cdh1)) ubiquitin ligase. The influence of Trim39 on MOAP-1 levels stems from the ability of Trim39 (a RING domain E3 ligase) to directly inhibit APC/C(Cdh1)-mediated protein ubiquitylation. Accordingly, small interfering ribonucleic acid-mediated knockdown of Cdh1 stabilized MOAP-1, thereby enhancing etoposide-induced Bax activation and apoptosis. These data identify Trim39 as a novel APC/C regulator and provide an unexpected link between the APC/C and apoptotic regulation via MOAP-1. | |
dc.identifier | ||
dc.identifier | jcb.201111141 | |
dc.identifier.eissn | 1540-8140 | |
dc.identifier.uri | ||
dc.language | eng | |
dc.publisher | Rockefeller University Press | |
dc.relation.ispartof | J Cell Biol | |
dc.relation.isversionof | 10.1083/jcb.201111141 | |
dc.subject | Adaptor Proteins, Signal Transducing | |
dc.subject | Adenomatous Polyposis Coli Protein | |
dc.subject | Apoptosis | |
dc.subject | Apoptosis Regulatory Proteins | |
dc.subject | Blotting, Western | |
dc.subject | Cadherins | |
dc.subject | Carrier Proteins | |
dc.subject | DNA Damage | |
dc.subject | Flow Cytometry | |
dc.subject | G1 Phase | |
dc.subject | HeLa Cells | |
dc.subject | Humans | |
dc.subject | Immunoprecipitation | |
dc.subject | RNA, Small Interfering | |
dc.subject | Recombinant Proteins | |
dc.subject | Ubiquitin | |
dc.subject | Ubiquitination | |
dc.subject | bcl-2-Associated X Protein | |
dc.title | The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1. | |
dc.type | Journal article | |
pubs.author-url | ||
pubs.begin-page | 361 | |
pubs.end-page | 367 | |
pubs.issue | 3 | |
pubs.organisational-group | Basic Science Departments | |
pubs.organisational-group | Duke | |
pubs.organisational-group | Duke Cancer Institute | |
pubs.organisational-group | Institutes and Centers | |
pubs.organisational-group | Pharmacology & Cancer Biology | |
pubs.organisational-group | School of Medicine | |
pubs.publication-status | Published | |
pubs.volume | 197 |
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