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http://purl.uniprot.org/citations/29020630http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29020630http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29020630http://www.w3.org/2000/01/rdf-schema#comment"We describe a mechanism by which the anti-apoptotic B cell lymphoma 2 (Bcl-2) protein is downregulated to induce apoptosis. ARTS (Sept4_i2) is a tumor suppressor protein that promotes cell death through specifically antagonizing XIAP (X-linked inhibitor of apoptosis). ARTS and Bcl-2 reside at the outer mitochondrial membrane in living cells. Upon apoptotic induction, ARTS brings XIAP and Bcl-2 into a ternary complex, allowing XIAP to promote ubiquitylation and degradation of Bcl-2. ARTS binding to Bcl-2 involves the BH3 domain of Bcl-2. Lysine 17 in Bcl-2 serves as the main acceptor for ubiquitylation, and a Bcl-2 K17A mutant has increased stability and is more potent in protection against apoptosis. Bcl-2 ubiquitylation is reduced in both XIAP- and Sept4/ARTS-deficient MEFs, demonstrating that XIAP serves as an E3 ligase for Bcl-2 and that ARTS is essential for this process. Collectively, these results suggest a distinct model for the regulation of Bcl-2 by ARTS-mediated degradation."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2017.09.052"xsd:string
http://purl.uniprot.org/citations/29020630http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2017.09.052"xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kim H.T."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kim H.T."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kagan J."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kagan J."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Chorubczyk N."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Chorubczyk N."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Curtz Y."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Curtz Y."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Edison N."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Edison N."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Haviv-Reingewertz T."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Haviv-Reingewertz T."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kfir N."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kfir N."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kupervaser M."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Kupervaser M."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Larisch S."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Larisch S."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Mamriev D."xsd:string
http://purl.uniprot.org/citations/29020630http://purl.uniprot.org/core/author"Mamriev D."xsd:string