{"database":"GEO","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://ftp.ncbi.nlm.nih.gov/geo/series/GSE282nnn/GSE282898/"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"omics_type":["Transcriptomics"],"species":["Homo sapiens"],"gds_type":["Expression profiling by high throughput sequencing"],"full_dataset_link":["https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE282898"],"repository":["GEO"],"entry_type":["GSE"],"additional_accession":[]},"is_claimable":false,"name":"N4BP1 RNase uses tandem KH domains to associate with EDC4 and mRNA decapping factors in P-bodies","description":"Processing (P)-bodies are non-membrane cellular structures containing proteins involved in mRNA decay. The enhancer of mRNA decapping protein 4 (EDC4) acts as a scaffold for the formation of the mRNA decapping complex in P-bodies. We show that NEDD4-binding partner-1 (N4BP1) interacts with EDC4 and with the DCP1A and XRN1 proteins involved in the hydrolysis of the mRNA 5′-cap structure in P-bodies. The two tandem KH domains (KHDs), KH-1 and KH-2, present in N4BP1 are essential for its interaction with EDC4. A crystal structure of the tandem KHDs revealed a typical type-I KH topology for both KH domains of N4BP1, and assembly into a globular fold. The N4BP1 KHDs lack the canonical GXXG motif necessary for interaction with single-stranded nucleic acids. The deletion of KH-1, both KHDs, or mutation in the existing non-canonical GXXG motifs in KHDs abolish N4BP1’s interaction with EDC4, indicating that both domains are mandatory for interaction with EDC4.","dates":{"publication":"2026/09/18"},"accession":"GSE282898","cross_references":{"GSM":["GSM8652369","GSM8652374","GSM8652371","GSM8652370","GSM8652373","GSM8652372"],"GPL":["29480"],"GSE":["282898"],"taxon":["Homo sapiens"],"PMID":["[42754686]"]}}