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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.identifier http://www.ncbi.nlm.nih.gov/pubmed/22529100
dc.identifier jcb.201111141
dc.identifier.uri https://hdl.handle.net/10161/8382
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.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
duke.contributor.id Zhang, Liguo|0520278
duke.contributor.id Kornbluth, Sally|0098545
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/22529100
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
dc.identifier.eissn 1540-8140


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