Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular basis of polyadenylated RNA fate determination in the nucleus.
Journal, issue, pages	Nature, Vol. 655, Issue 8124, Page 1070-1078, Year 2026
Publish date	Jun 17, 2026
Authors	Andrii Bugai / Ulrich Hohmann / Ana Lorenzo / Max Graf / Laura Fin / Jérôme O Rouvière / Laszlo Tirian / Yuhui Dou / Marion Le Rest / Patrik Polák / Dennis Johnsen / Lis Jakobsen / Jens Skorstengaard Andersen / Julius Brennecke / Clemens Plaschka / Torben Heick Jensen /
PubMed Abstract	Eukaryotic genomes generate a plethora of polyadenylated (pA) RNAs, which are packaged into ribonucleoprotein particles (RNPs). To ensure faithful gene expression, functional pA RNPs, including ...Eukaryotic genomes generate a plethora of polyadenylated (pA) RNAs, which are packaged into ribonucleoprotein particles (RNPs). To ensure faithful gene expression, functional pA RNPs, including protein-coding RNPs, are exported to the cytoplasm, whereas transcripts within non-functional pA RNPs are degraded in the nucleus. How cells distinguish these opposing fates remains unknown. The DExD-box ATPase UAP56 (also known as DDX39B) is a central component of functional pA RNPs, and promotes their docking to the nuclear pore complex-anchored TREX-2, which triggers transcript release from UAP56 to facilitate export. Here we reveal that the poly(A) tail exosome targeting (PAXT) connection binds a TREX-2-like module, which releases pA RNAs from UAP56 for decay by the nuclear exosome. The core of this module consists of a LENG8-PCID2-SEM1 trimer, which we show is structurally and biochemically equivalent to the central GANP-PCID2-SEM1 trimer of TREX-2. Mutagenesis and transcriptomic data demonstrate that the nuclear fate of pA RNPs is governed by the contending actions of nucleoplasmic PAXT and nuclear pore complex-associated TREX-2, which interpret RNA-bound UAP56 as a signal for RNA decay or export, respectively. As RNA targets of PAXT are generally short and intron-poor, we propose an overall model for pA RNP fate determination whereby the distinct sub-nuclear localizations of PAXT and TREX-2 govern the degradation of short non-functional pA RNAs while allowing export of their longer and functional counterparts.
External links	Nature / PubMed:42310446 / PubMed Central
Methods	EM (single particle)
Resolution	2.62 - 6.2 Å
Structure data	54282 9rv1 EMDB-54282, PDB-9rv1: Cryo-EM structure of the human UAP56-RNA - SAC3D1-PCID2-SEM1 complex Method: EM (single particle) / Resolution: 2.62 Å EMDB-54283: Human UAP56-RNA - SAC3D1-PCID2-SEM1 complex, Map A Method: EM (single particle) / Resolution: 2.88 Å EMDB-54284: Map B of the human UAP56-RNA - SAC3D1-PCID2-SEM1 complex Method: EM (single particle) / Resolution: 2.62 Å 56930 28wy EMDB-56930, PDB-28wy: Cryo-EM structure of the human SAC3D1-PCID2-SEM1 complex Method: EM (single particle) / Resolution: 3.6 Å 56931 28wz EMDB-56931, PDB-28wz: Cryo-EM structure of the human LENG8-PCID2-SEM1 complex Method: EM (single particle) / Resolution: 3.5 Å 56932 28xa EMDB-56932, PDB-28xa: Cryo-EM structure of the human UAP56 NTD - LENG8-PCID2-SEM1 complex Method: EM (single particle) / Resolution: 4.86 Å 56933 28xb EMDB-56933, PDB-28xb: Cryo-EM structure of the human UAP56-RNA - LENG8-PCID2-SEM1 complex Method: EM (single particle) / Resolution: 6.2 Å
Chemicals	ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry ChemComp-HOH*: WATER
Source	homo sapiens (human) escherichia coli (E. coli)
Keywords	GENE REGULATION / mRNA export