| http://purl.uniprot.org/citations/19100260 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19100260 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19100260 | http://www.w3.org/2000/01/rdf-schema#comment | "Bax, a multi-domain pro-apoptotic Bcl-2 family member, is a key regulator for the release of apoptogenic factors from mitochondria. MOAP-1, which was first isolated from a screen for Bax-associating proteins, interacts with Bax upon apoptotic induction. MOAP-1 is a short-lived protein that is constitutively degraded by the ubiquitin-proteasome system. Apoptotic stimuli upregulate MOAP-1 rapidly through inhibition of its poly-ubiquitination process. However, cellular factors that regulate the stability of MOAP-1 have not yet been identified. In this study, we report the identification of TRIM39 as a MOAP-1-binding protein. TRIM39 belongs to a family of proteins characterized by a Tripartite Motif (TRIM), consisting of RING domain, B-box and coiled-coil domain. Several TRIM family members are known to demonstrate E3 ubiquitin ligase activity. Surprisingly, TRIM39 significantly extends the half-life of MOAP-1 by inhibiting its poly-ubiquitination process. In agreement with its effect on enhancing MOAP-1 stability, TRIM39 sensitizes cells to etoposide-induced apoptosis. Conversely, knockdown of TRIM39 reduces the sensitivity of cells to etoposide-stimulated apoptosis. Furthermore, TRIM39 elevates the level of MOAP-1 in mitochondria and promotes cytochrome c release from isolated mitochondria stimulated by recombinant Bax. Together, these data suggest that TRIM39 can promote apoptosis signalling through stabilization of MOAP-1."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.yexcr.2008.11.021"xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.yexcr.2008.11.021"xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Lee S.S."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Lee S.S."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Wan Q."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Wan Q."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Fu N.Y."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Fu N.Y."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Sukumaran S.K."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Sukumaran S.K."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Yu V.C."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Yu V.C."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Wan K.F."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/author | "Wan K.F."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/name | "Exp. Cell Res."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/name | "Exp. Cell Res."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/pages | "1313-1325"xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/pages | "1313-1325"xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/title | "TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process."xsd:string |
| http://purl.uniprot.org/citations/19100260 | http://purl.uniprot.org/core/title | "TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process."xsd:string |