GEOapplication/xmlftp://ftp.ncbi.nlm.nih.gov/geo/series/GSE282nnn/GSE282898/primaryOK200TranscriptomicsHomo sapiensExpression profiling by high throughput sequencinghttps://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE282898GEOGSEfalseN4BP1 RNase uses tandem KH domains to associate with EDC4 and mRNA decapping factors in P-bodiesProcessing (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 EDC4.2026/09/18GSE282898GSM8652369GSM8652374GSM8652371GSM8652370GSM8652373GSM865237229480282898Homo sapiens[42754686]