http://purl.uniprot.org/citations/21981923 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21981923 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21981923 | http://www.w3.org/2000/01/rdf-schema#comment | "miRNAs are posttranscriptional regulators of gene expression that associate with Argonaute and GW182 proteins to repress translation and/or promote mRNA degradation. miRNA-mediated mRNA degradation is initiated by deadenylation, although it is not known whether deadenylases are recruited to the mRNA target directly or by default, as a consequence of a translational block. To answer this question, we performed a screen for potential interactions between the Argonaute and GW182 proteins and subunits of the two cytoplasmic deadenylase complexes. We found that human GW182 proteins recruit the PAN2-PAN3 and CCR4-CAF1-NOT deadenylase complexes through direct interactions with PAN3 and NOT1, respectively. These interactions are critical for silencing and are conserved in D. melanogaster. Our findings reveal that GW182 proteins provide a docking platform through which deadenylase complexes gain access to the poly(A) tail of miRNA targets to promote their deadenylation, and they further indicate that deadenylation is a direct effect of miRNA regulation."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2011.09.007"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2011.09.007"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Izaurralde E."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Izaurralde E."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Braun J.E."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Braun J.E."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Fauser M."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Fauser M."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Huntzinger E."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/author | "Huntzinger E."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/pages | "120-133"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/pages | "120-133"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/title | "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/title | "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/volume | "44"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://purl.uniprot.org/core/volume | "44"xsd:string |
http://purl.uniprot.org/citations/21981923 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21981923 |
http://purl.uniprot.org/citations/21981923 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21981923 |