| http://purl.uniprot.org/citations/21610068 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21610068 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21610068 | http://www.w3.org/2000/01/rdf-schema#comment | "Inositol 1,4,5-trisphosphate (IP(3)) receptors are endoplasmic reticulum membrane calcium channels that, upon activation, are degraded via the ubiquitin-proteasome pathway. While searching for novel mediators of IP(3) receptor processing, we discovered that RNF170, an uncharacterized RING domain-containing protein, associates rapidly with activated IP(3) receptors. RNF170 is predicted to have three membrane-spanning helices, is localized to the ER membrane, and possesses ubiquitin ligase activity. Depletion of endogenous RNF170 by RNA interference inhibited stimulus-induced IP(3) receptor ubiquitination, and degradation and overexpression of a catalytically inactive RNF170 mutant suppressed stimulus-induced IP(3) receptor processing. A substantial proportion of RNF170 is constitutively associated with the erlin1/2 (SPFH1/2) complex, which has been shown previously to bind to IP(3) receptors immediately after their activation. Depletion of RNF170 did not affect the binding of the erlin1/2 complex to stimulated IP(3) receptors, whereas erlin1/2 complex depletion inhibited RNF170 binding. These results suggest a model in which the erlin1/2 complex recruits RNF170 to activated IP(3) receptors where it mediates IP(3) receptor ubiquitination. Thus, RNF170 plays an essential role in IP(3) receptor processing via the ubiquitin-proteasome pathway."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.251983"xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.251983"xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Lu J.P."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Lu J.P."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Sliter D.A."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Sliter D.A."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Wojcikiewicz R.J."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Wojcikiewicz R.J."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Pearce M.M."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/author | "Pearce M.M."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/pages | "24426-24433"xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/pages | "24426-24433"xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/title | "RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/title | "RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation."xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/volume | "286"xsd:string |
| http://purl.uniprot.org/citations/21610068 | http://purl.uniprot.org/core/volume | "286"xsd:string |