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| Item Type: | Article |
|---|---|
| Title: | N4BP1 uses tandem KH domains to associate with EDC4 and mRNA decapping factors in P-bodies |
| Creators: |
Piłat, Paweł, Garg, Ankur  ORCID: https://orcid.org/0000-0003-2397-1670, Heinemann, Udo ORCID: https://orcid.org/0000-0002-8191-3850, Wilamowski, Mateusz and Jura, Jolanta
|
| Abstract: | Processing bodies (P-bodies) are cytoplasmic, non-membrane-bound structures involved in mRNA decay. EDC4 serves as a key scaffold for the decapping complex within P-bodies. Here, we demonstrate that N4BP1 interacts with EDC4, as well as with DCP1A, DCP2, and XRN1 - key components of 5′-cap hydrolysis. Endogenous N4BP1 colocalizes with EDC4 in P-bodies, requiring both of its KH domains. Structural analysis revealed that N4BP1 contains a type-I KH fold but lacks the canonical GXXG motif required for single-stranded RNA binding. Deletion or mutation of KH domains non-canonical GXXG motifs disrupts the N4BP1-EDC4 complex. N4BP1 reduces HIV-1 transcript levels independently of its P-body localization or association with decapping components, implying the involvement of other host factors in regulating viral mRNAs. Similarly, for N4PB1-dependend negative regulation of endogenous transcripts in HaCaT keratinocytes, EDC4 is not essential. For both HIV-1 and endogenous transcripts, the reduction is associated with the activity of the NYN domain. |
| Keywords: | Endoribonucleases, Exoribonucleases, HEK293 Cells, HIV-1, HaCaT Cells, Messenger RNA, Microtubule-Associated Proteins, Processing Bodies, Protein Binding, Protein Domains, Proteins, RNA Caps, RNA Recognition Motif Proteins, RNA Stability, RNA-Binding Proteins, Trans-Activators |
| Source: | Communications Biology |
| ISSN: | 2399-3642 |
| Publisher: | Nature Publishing Group |
| Volume: | 9 |
| Number: | 1 |
| Page Range: | 1215 |
| Date: | 17 September 2026 |
| Official Publication: | https://doi.org/10.1038/s42003-026-10938-x |
| PubMed: | View item in PubMed |
| Related to: |
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