| http://purl.uniprot.org/citations/21220307 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21220307 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21220307 | http://www.w3.org/2000/01/rdf-schema#comment | "Cyclin-dependent kinase 5 (Cdk5) is an atypical but essential member of the Cdk kinase family, and its dysregulation or deletion has been implicated in inflammation-related disorders by an undefined mechanism. Here we show that Cdk5 is an indispensable activator of the GAIT (IFN-γ-activated inhibitor of translation) pathway, which suppresses expression of a posttranscriptional regulon of proinflammatory genes in myeloid cells. Through induction of its regulatory protein, Cdk5R1 (p35), IFN-γ activates Cdk5 to phosphorylate Ser(886) in the linker domain of glutamyl-prolyl tRNA synthetase (EPRS), the initial event in assembly of the GAIT complex. Cdk5/p35 also induces, albeit indirectly via a distinct kinase, phosphorylation of Ser(999), the second essential event in GAIT pathway activation. Diphosphorylated EPRS is released from its residence in the tRNA multisynthetase complex for immediate binding to NS1-associated protein and subsequent binding to ribosomal protein L13a and GAPDH. The mature heterotetrameric GAIT complex binds the 3' UTR GAIT element of VEGF-A and other target mRNAs and suppresses their translation in myeloid cells. Inhibition of Cdk5/p35 inhibits both EPRS phosphorylation events, prevents EPRS release from the tRNA multisynthetase complex, and blocks translational suppression of GAIT element-bearing mRNAs, resulting in increased expression of inflammatory proteins. Our study reveals a unique role of Cdk5/p35 in activation of the major noncanonical function of EPRS, namely translational control of macrophage inflammatory gene expression."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1011275108"xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1011275108"xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Jia J."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Jia J."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "DiCorleto P.E."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "DiCorleto P.E."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Fox P.L."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Fox P.L."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Arif A."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Arif A."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Moodt R.A."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/author | "Moodt R.A."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/pages | "1415-1420"xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/pages | "1415-1420"xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/title | "Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational control."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/title | "Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational control."xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/volume | "108"xsd:string |
| http://purl.uniprot.org/citations/21220307 | http://purl.uniprot.org/core/volume | "108"xsd:string |