9T6L
Cryo-EM structure of the human LENG8-PCID2-DSS1 complex bound to UAP56 and RRP1B
Summary for 9T6L
| Entry DOI | 10.2210/pdb9t6l/pdb |
| EMDB information | 55617 |
| Descriptor | Spliceosome RNA helicase DDX39B, Leukocyte receptor cluster member 8,Ribosomal RNA processing protein 1 homolog B, PCI domain-containing protein 2, ... (4 entities in total) |
| Functional Keywords | rna metabolism, rna decay, splicing quality control, nuclear protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 135009.08 |
| Authors | Abbas, D.K.,Bonneau, F.,Basquin, J.,Conti, E.,Schussler, S.,Wilkinson, M.E. (deposition date: 2025-11-07, release date: 2026-05-27) |
| Primary citation | Abbas, D.K.,Bonneau, F.,Wilkinson, M.E.,Schussler, S.,Basquin, J.,Conti, E. Evolutionarily conserved spliceosome-exosome pathway in nuclear mRNA surveillance. Genes Dev., 2026 Cited by PubMed Abstract: Intron-containing mRNAs are cotranscriptionally spliced and assembled into messenger ribonucleoprotein (mRNP) particles, a process monitored by surveillance pathways. Here, we combined biochemical and structural approaches to elucidate the mechanisms by which mRNPs are sorted between two opposing fates: nuclear degradation and cytoplasmic export. While the human GANP-PCID2 complex is known to connect mRNPs to nuclear export, our data indicate that the LENG8-PCID2 complex operates as an mRNP decay connector, coupling nuclear mRNPs to the RNA-degrading exosome via the PAXT adaptor complex. Both recognize the mRNP component UAP56, but LENG8-PCID2 uniquely associates with early splicing factors through a direct interaction with U1A and RRP1B. Similarly, the Thp3-Csn12 ortholog in budding yeast couples the early splicing factors Mud2-Bbp with the nuclear exosome. The spliceosome-exosome mRNP decay pathway we uncovered reveals molecular principles that remain strikingly conserved across evolution, despite the fundamental differences in splicing and decay between humans and budding yeast. PubMed: 42140674DOI: 10.1101/gad.353594.125 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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