Affinage

UPF2

Regulator of nonsense transcripts 2 · UniProt Q9HAU5

Length
1272 aa
Mass
147.8 kDa
Annotated
2026-06-10
37 papers in source corpus 22 papers cited in narrative 24 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

UPF2 is a central scaffold of the nonsense-mediated mRNA decay (NMD) pathway, physically bridging the surveillance factors UPF3b and UPF1 and acting as the conformational switch that activates UPF1 once a premature termination event is recognized (PMID:18066079, PMID:11113196). Through its modular MIF4G domains it organizes a heptameric surveillance complex assembled on RNA with the exon-junction complex core, in which UPF3b is bridged from the EJC to UPF1, and UPF2/UPF3b cooperatively stimulate the ATPase and helicase activities of UPF1 (PMID:18066079). Structurally, the UPF2 MIF4G-3 domain engages the UPF3b RNP/NOPS-L surface through an intimate, conserved interface, while MIF4G-1 and MIF4G-2 provide an essential scaffolding role and MIF4G-3 together with the UPF1-binding region constitutes the minimal NMD-triggering module (PMID:15004547, PMID:24271394, PMID:35640974). UPF2 binds the UPF1 cysteine-histidine-rich (CH) domain, and this contact drives a large conformational change in UPF1 that converts it from an RNA-clamping state to an RNA-unwinding state while allosterically lowering UPF1's RNA affinity to release bound RNA (PMID:21419344, PMID:16931876, PMID:36456182). Beyond scaffolding, UPF2 is itself a nucleic-acid-binding protein: its MIF4G-1 and MIF4G-3 modules bind and stabilize single-stranded RNA and MIF4G-3 possesses RNA annealing activity, allowing full-length UPF2 to unfold structured RNA (PMID:40246535). UPF2 also serves as a substrate and docking site for the SMG1 kinase complex, which recruits UPF1 and UPF2 to distinct sites and transfers UPF2 onto UPF1 to activate it, and it contacts the eukaryotic release factor eRF3 and the SURF complex at terminating ribosomes through its C-terminal region that overlaps the UPF3b site (PMID:24271394, PMID:25002321, PMID:26740584). By occupying the UPF1 CH domain, UPF2 competes with the SMG6 endonuclease and the decapping enzyme Dcp2, placing it at the center of mutually exclusive UPF1-containing complexes that partition surveillance from degradation (PMID:38709891). Loss of UPF2 stabilizes PTC-bearing transcripts and other NMD substrates, and the UPF2-UPF1 interaction is essential for viability and for decay of most targets (PMID:21317294, PMID:11889124).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2001 Medium

    Established UPF2 as a physical hub of the human NMD machinery by defining its direct, domain-specific contacts with UPF1 and UPF3b and its predominantly cytoplasmic localization.

    Evidence Reciprocal Co-IP of epitope-tagged proteins with deletion mapping and immunofluorescence in HeLa cells

    PMID:11113196

    Open questions at the time
    • Did not resolve the structural basis of the interactions
    • Did not determine the functional consequence of complex assembly on UPF1 activity
  2. 2002 Medium

    Demonstrated that UPF2 is functionally required for NMD by showing its depletion stabilizes PTC-bearing transcripts in a translation-dependent manner.

    Evidence Antisense hUPF2 knockdown with TCR-beta PTC reporters, fractionation, and translation-initiation inhibition; yeast UPF2 deletion with CPA1 uORF reporters

    PMID:11889124 PMID:12172963

    Open questions at the time
    • Did not define how UPF2 promotes decay biochemically
    • Did not identify the degradation machinery engaged downstream
  3. 2004 High

    Resolved the molecular basis of the UPF2-UPF3b interaction, showing UPF3b uses its RNP surface for protein contact while UPF2 retains RNA binding.

    Evidence 1.95 A crystal structure of UPF2 MIF4G domain bound to UPF3b RNP with RNA-binding and mutational assays

    PMID:15004547

    Open questions at the time
    • Did not address how this interface positions UPF1
    • Did not establish the role of other MIF4G domains
  4. 2006 High

    Defined the UPF1 CH domain structure and identified the surfaces it uses to bind UPF2, the contact later shown to be a competitive hub.

    Evidence 3 A crystal structure of the UPF1 CH domain with site-directed mutagenesis and binding assays

    PMID:16931876

    Open questions at the time
    • Did not show the conformational consequence of UPF2 binding
    • Did not address competition with other CH-domain partners
  5. 2007 High

    Reconstituted the activating mechanism, showing UPF2 and UPF3b cooperatively stimulate UPF1 ATPase and helicase activity within an EJC-bridged surveillance complex.

    Evidence In vitro reconstitution of recombinant EJC core plus UPF1/2/3b on RNA with ATPase and helicase assays

    PMID:18066079

    Open questions at the time
    • Did not provide a structural mechanism for the activation
    • Did not establish how this couples to downstream decay
  6. 2011 High

    Provided the structural mechanism of UPF1 activation, showing UPF2 binding triggers a CH-domain conformational change that switches UPF1 from RNA-clamping to RNA-unwinding.

    Evidence Crystal structures of Upf1 with transition-state analogue and RNA, with and without CH domain, plus ATPase/helicase assays

    PMID:21419344

    Open questions at the time
    • Did not quantify the effect on RNA affinity
    • Did not place the switch within the full SMG1-coupled pathway
  7. 2013 High

    Dissected the modular architecture of UPF2, assigning scaffolding to MIF4G-1/2 and the NMD-triggering function plus SMG1 substrate role to MIF4G-3.

    Evidence Crystal structures of MIF4G-1 and MIF4G-2, in vitro SMG1 kinase and complex-assembly assays, and in vivo complementation/tethering

    PMID:24271394

    Open questions at the time
    • Did not determine the consequence of MIF4G-3 phosphorylation
    • Did not define MIF4G-1/2 binding partners that explain the scaffolding role
  8. 2014 Medium

    Linked UPF2 to the SMG1 kinase complex, showing it docks on SMG1 independently of UPF1 and is transferred to UPF1 to activate it, and identified a UPF3-independent scaffolding region.

    Evidence EM of SMG1C with in vivo/in vitro interaction and competition assays; yeast Upf2 N-terminal mIF4G crystal structure with NMD assays and Dbp6 Co-IP

    PMID:25002321 PMID:25277656

    Open questions at the time
    • Did not resolve the order of events during in-cell activation
    • Mechanism of UPF2 transfer within SMG1C not structurally defined
  9. 2016 Medium

    Connected UPF2 to translation termination by demonstrating direct binding to eRF3 and ribosome/SURF association through a C-terminal region overlapping the UPF3b site.

    Evidence Biochemical binding assays, EM of UPF2-eRF3, deletion mapping, and in-cell Co-IP

    PMID:26740584

    Open questions at the time
    • Did not establish the in vivo timing of eRF3 versus UPF3b engagement
    • Functional consequence of eRF3 binding for NMD not directly tested
  10. 2022 High

    Refined the activation mechanism by showing UPF2 binding allosterically lowers UPF1 RNA affinity to release RNA, and resolved how UPF3 isoform binding competition and a disease mutation tune the UPF2 interface.

    Evidence Fluorescence anisotropy/filter binding RNA-release assays; crystal and cryo-EM structures of MIF4GIII with UPF3B/UPF3A and ITC affinity measurements with mutagenesis

    PMID:35640974 PMID:36456182

    Open questions at the time
    • Did not link RNA release timing to substrate commitment in cells
    • Functional outcome of UPF3A/UPF3B competition on target selection not fully resolved
  11. 2024 High

    Established UPF2 as the determinant of mutually exclusive UPF1 complexes by showing SMG6 binds the same CH domain as UPF2, partitioning surveillance from endonucleolytic decay.

    Evidence Mass spectrometry, cryo-EM, and biochemical competition/mutagenesis assays

    PMID:38709891

    Open questions at the time
    • Did not define the in-cell trigger that switches between complexes
    • Conformational coupling to UPF1 RNA status inferred rather than directly imaged
  12. 2025 Medium

    Characterized UPF2 as an intrinsic RNA-binding/remodeling protein and extended its role to histone mRNA decay and viral antagonism, while implicating Dcp2 competition for the UPF1 CH domain.

    Evidence Nucleic-acid binding/annealing/unfolding assays with domain mapping; recombinant interaction and helicase assays for 3'hExo/SLBP; binding and NMD reporter assays for SARS-CoV-2 Np; recombinant competition assays for Dcp2 (preprint)

    PMID:39831305 PMID:40246535

    Open questions at the time
    • 3'hExo and Dcp2 findings rest on preprint/single-lab biochemistry awaiting peer-reviewed confirmation
    • In-cell relevance of UPF2 RNA-remodeling activity not established
    • Mechanism by which viral Np outcompetes UPF1 in vivo not resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the competing UPF2-, SMG6-, and Dcp2-containing UPF1 complexes are temporally ordered and switched in cells to commit a transcript to decay remains unresolved.
  • No in-cell measurement of complex exchange kinetics
  • No structure of the complete surveillance-to-decay transition
  • Regulation of UPF2 stability and its impact on pathway flux not mechanistically defined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3 GO:0003723 RNA binding 2 GO:0140098 catalytic activity, acting on RNA 1
Localization
GO:0005634 nucleus 1 GO:0005829 cytosol 1
Pathway
R-HSA-8953854 Metabolism of RNA 3
Partners
DCP2ETF3H (ERF3)RBM8ASMG1SMG6UPF1UPF3AUPF3B
Complex memberships
NMD surveillance complex (UPF1-UPF2-UPF3b)SMG1C (SMG1-SMG8-SMG9)SURF complexexon junction complex (EJC core)

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2007 UPF2 and UPF3b cooperatively stimulate both ATPase and RNA helicase activities of UPF1 within a heptameric complex assembled on RNA with the EJC core (eIF4AIII, MAGOH, Y14). The EJC proteins provide a composite binding site for UPF3b that bridges to UPF2 and UPF1. In vitro reconstitution of recombinant EJC core + UPF1/2/3b complex on RNA; ATPase and helicase activity assays Nature structural & molecular biology High 18066079
2011 Crystal structures of Upf1 with and without its CH domain reveal that in isolation Upf1 clamps onto RNA. Upon UPF2 binding, the regulatory CH domain of Upf1 undergoes a large conformational change that causes the catalytic helicase domain to bind RNA less extensively, switching Upf1 from an RNA-clamping mode to an RNA-unwinding mode. Crystal structures of Upf1 with ADP:AlF4⁻ and RNA (transition-state analogue), with and without CH domain; biochemical ATPase/helicase assays Molecular cell High 21419344
2001 Human UPF2 interacts with hUPF1, hUPF3b-X, and hUPF3 via defined protein domains. hUPF2 localizes primarily to the cytoplasm (with hUPF1), while hUPF3b-X localizes primarily to nuclei and shuttles. Co-immunoprecipitation of epitope-tagged proteins in HeLa cells; indirect immunofluorescence; domain mapping by deletion constructs Molecular and cellular biology Medium 11113196
2004 Crystal structure of the UPF2 MIF4G domain in complex with the UPF3b RNP domain at 1.95 Å reveals that the protein-protein interface is mediated by highly conserved charged residues; the UPF3b RNP beta-sheet surface (normally used for nucleic acid binding) is used for protein-protein interaction and does not bind RNA, whereas UPF2 retains RNA-binding capacity. X-ray crystallography (1.95 Å); RNA binding assays; mutational analysis Nature structural & molecular biology High 15004547
2005 CBP80 interacts with UPF1 and promotes the interaction of UPF1 with UPF2 during NMD of CBP80-bound (pioneer round) mRNAs, but does not promote UPF1 interaction with Staufen1 in SMD. Co-immunoprecipitation in mammalian cells; NMD reporter assays; siRNA knockdown Nature structural & molecular biology Medium 16186820
2006 Crystal structure (3 Å) of the UPF1 cysteine-histidine-rich (CH) domain reveals a unique combination of three zinc-binding motifs in two tandem modules related to RING-box and U-box domains. Mutational analysis identifies two distinct conserved surface regions of UPF1 CH domain that mediate interaction with UPF2. X-ray crystallography (3 Å); site-directed mutagenesis; binding assays RNA (New York, N.Y.) High 16931876
2013 Crystal structures of UPF2 MIF4G-1 and MIF4G-2 show N-terminal capping helices essential for MIF4G core stabilization; MIF4G-2 interacts with MIF4G-3, forming a rigid assembly. MIF4G-3 is the binding site and in vitro substrate of SMG1 kinase, and a ternary UPF2 MIF4G-3/UPF3b/SMG1 complex forms in vitro. MIF4G-1 and MIF4G-2 have an essential scaffolding role for NMD, while MIF4G-3 plus the UPF1-binding region is the minimal module required to trigger NMD. Crystal structures; in vitro kinase assay (SMG1 phosphorylation of UPF2 MIF4G-3); in vitro complex assembly; in vivo complementation assays; tethering assays Nucleic acids research High 24271394
2014 SMG1C (SMG1-SMG8-SMG9) recruits UPF1 and UPF2 to distinct sites near the kinase domain. UPF2 binds SMG1 at its FRB domain in a UPF1-independent manner. UPF2 can be transferred to UPF1 within SMG1C, inducing UPF2-dependent conformational changes that activate UPF1 within an SMG1C-UPF1-UPF2 complex. Electron microscopy; in vivo and in vitro interaction analyses; competition experiments; mutagenesis Structure Medium 25002321
2014 Crystal structure of the N-terminal mIF4G domain of yeast Upf2 reveals a highly conserved region essential for NMD that is independent of Upf2 binding sites for Upf1 and Upf3. Mutations in this region inactivate NMD and disrupt Upf2 binding to Dbp6, a DEAD-box helicase, suggesting Upf2 acts as a platform for additional NMD factors. X-ray crystallography; site-directed mutagenesis; NMD functional assays; co-immunoprecipitation Journal of molecular biology Medium 25277656
2016 UPF2 directly interacts with eukaryotic release factor eRF3, associates with the SURF complex and ribosomes in cells in a UPF3-independent manner. The eRF3 binding site maps to the C-terminal part of UPF2, overlapping partially with the UPF3b-binding site. UPF2 binds UPF3b more strongly than eRF3, and UPF3b interaction interferes with UPF2-eRF3 complex assembly. Biochemical binding assays; electron microscopy of UPF2-eRF3 complex; deletion mapping; co-immunoprecipitation from cells Nucleic acids research Medium 26740584
2002 In yeast, deletion of UPF2 (or UPF1 and UPF3) enhances synthesis of CPSase A encoded by CPA1, an effect that depends on the presence of the CPA1 uORF, showing that the NMD complex destabilizes the 5' end of the CPA1 mRNA and that NMD cooperates with arginine-mediated translational repression. Yeast genetic deletion analysis; enzymatic activity assays; reporter assays with uORF mutants Current genetics Medium 12172963
2006 Upf1 and Upf2 associate with NMD-sensitive AUF1 3'-UTR splice variant mRNAs in cells (RNP immunoprecipitation). Knockdown of Upf1/Upf2 by RNAi specifically stabilizes NMD-sensitive AUF1 mRNA variants containing exon-exon junctions >50 nt downstream of the stop codon, providing evidence that NMD and ARE-mediated decay pathways are linked. siRNA knockdown of Upf1/Upf2; RT-qPCR mRNA stability assays; RNP immunoprecipitation; dominant-negative Upf1 transfection Molecular and cellular biology Medium 17000771
2011 In Drosophila, loss-of-function of upf1 and upf2 inhibits cell growth and induces apoptosis through a Upf3-independent pathway. A mutant Upf2 unable to bind Upf3 still causes lethality, while disruption of Upf2-Upf1 interaction causes death, indicating that the Upf2-Upf1 interaction (not Upf2-Upf3) is essential for viability and NMD of most targets. Drosophila loss-of-function genetics; epistasis analysis with upf3 mutants; Upf2 binding-domain mutants; cell growth and apoptosis assays RNA (New York, N.Y.) Medium 21317294
2022 Binding of UPF2 to UPF1 drastically reduces UPF1's affinity for RNA, causing release of bound RNA through an allosteric mechanism (not direct competition for RNA binding), mediated by the conformational change in UPF1 induced upon UPF2 binding. Biochemical binding assays (fluorescence anisotropy, filter binding); biophysical methods; in vitro RNA-release assays; mutational analysis RNA (New York, N.Y.) High 36456182
2022 Crystal and cryo-EM structures of UPF2 MIF4GIII in complex with UPF3B or UPF3A reveal unexpectedly intimate binding interfaces. UPF3B disease-causing mutation Y160D in the NOPS-L domain displaces Y160 from a hydrophobic cleft in UPF2, reducing binding affinity ~40-fold. UPF3A binds UPF2 with ~10-fold higher affinity than UPF3B via NOPS-L residues, explaining competitive binding and compensatory upregulation. X-ray crystallography and cryo-EM structures; isothermal titration calorimetry / binding affinity measurements; mutagenesis Nucleic acids research High 35640974
2024 The SMG6 endonuclease contains a conserved short linear motif that binds the UPF1 CH domain (the same domain that binds UPF2), making SMG6 and UPF2 binding to UPF1 mutually exclusive. Cryo-EM data suggest that distinct SMG6-containing and UPF2-containing NMD complexes are dictated by different conformational states linked to UPF1's RNA-binding status. Mass spectrometry; cryo-EM; biochemical interaction assays; competition experiments; mutagenesis Nucleic acids research High 38709891
2025 UPF2 binds RNA dynamically: MIF4G-1 and MIF4G-3 are the main RNA/DNA-binding modules; MIF4G-3 has RNA annealing activity; full-length UPF2 unfolds a reporter hairpin RNA structure. UPF2 preferentially binds and stabilizes single-stranded RNA in a sequence-independent manner and undergoes a conformational change upon ssRNA binding. Nucleic acid binding assays; RNA annealing/unfolding assays; biochemical and biophysical methods; domain deletion analysis RNA (New York, N.Y.) Medium 40246535
2025 UPF2 binds the exoribonuclease 3'hExo (involved in histone mRNA decay), and UPF2-mediated activation of UPF1 overrides the inhibitory effect of SLBP on UPF1's unwinding activity during histone mRNA degradation. Direct interaction assays (recombinant proteins); in vitro helicase/unwinding assays; functional mRNA decay assays in cells bioRxivpreprint Medium
2025 In yeast, Dcp2 and Upf2 compete for the same binding site in the Upf1 N-terminal CH domain, accounting for the existence of two mutually exclusive Upf1-containing complexes (Upf1-Upf2/3 surveillance complex and Upf1-decapping complex). Recombinant protein interaction assays; competition binding experiments; pulldowns bioRxivpreprint Medium
2025 SARS-CoV-2 nucleocapsid protein (Np) binds directly to UPF2, disrupting formation of the UPF1/UPF2 complex and negating the stimulatory effect of UPF2 on UPF1 catalytic activity, thereby inhibiting cellular NMD. Biochemical and biophysical binding assays; ATPase/helicase activity assays; cellular NMD reporter assays Nucleic acids research Medium 39831305
2016 Upf2 protein is present in both cytoplasmic and nucleoplasmic fractions of human cells. Upf2 interacts with the EJC core factor RBM8A (Y14) not only in the cytoplasm but also in the intranuclear region, as shown by proximity ligation assay. Subcellular fractionation; western blotting; immunofluorescence; in situ proximity ligation assay; RNase treatment Molecular medicine reports Low 27221324
2013 Proteasome inhibitors cause accumulation of UPF2 protein levels in cells; knockdown of SMG1 also upregulates UPF2 protein levels; these effects are additive, suggesting UPS and SMG1 regulate UPF2 protein stability via distinct pathways. Proteasome inhibitor treatment; siRNA knockdown of SMG1; western blotting International journal of oncology Low 24173962
2002 hUPF2-dependent NMD pathway operating in the nuclear fraction of cells is required for down-regulation of PTC-bearing TCR-beta transcripts; this requires translation features (initiator ATG, scanning) suggesting cytoplasmic ribosomes act on nuclear-associated mRNAs. Antisense hUPF2 knockdown; TCR-beta PTC reporter assays; nuclear/cytoplasmic fractionation; inhibition of translation initiation The Journal of biological chemistry Medium 11889124
2024 Chemical cross-linking mass spectrometry reveals that UPF2 acts as a connection bridge between SMG1 and SMG7 in the NMD machinery; UPF2 N-terminal forms most interactions with SMG7; MIF4G-I, II, and III domains contact SMG1 or SMG7. Chemical cross-linking mass spectrometry (CLMS); structural modeling International journal of molecular sciences Low 38542156

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity. Nature structural & molecular biology 274 18066079
2011 Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2. Molecular cell 238 21419344
2001 Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4). Molecular and cellular biology 208 11113196
1997 Molecular cloning and functional characterization of nitrobenzylthioinosine (NBMPR)-sensitive (es) and NBMPR-insensitive (ei) equilibrative nucleoside transporter proteins (rENT1 and rENT2) from rat tissues. The Journal of biological chemistry 187 9353301
2004 The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3. Nature structural & molecular biology 166 15004547
2005 CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells. Nature structural & molecular biology 126 16186820
2016 UPF2-Dependent Nonsense-Mediated mRNA Decay Pathway Is Essential for Spermatogenesis by Selectively Eliminating Longer 3'UTR Transcripts. PLoS genetics 78 27149259
2006 Crystal structure of the UPF2-interacting domain of nonsense-mediated mRNA decay factor UPF1. RNA (New York, N.Y.) 78 16931876
2014 Structures of SMG1-UPFs complexes: SMG1 contributes to regulate UPF2-dependent activation of UPF1 in NMD. Structure (London, England : 1993) 70 25002321
2010 UPF2 is a critical regulator of liver development, function and regeneration. PloS one 64 20657840
2002 A quality control pathway that down-regulates aberrant T-cell receptor (TCR) transcripts by a mechanism requiring UPF2 and translation. The Journal of biological chemistry 60 11889124
2019 Inhibition of Upf2-Dependent Nonsense-Mediated Decay Leads to Behavioral and Neurophysiological Abnormalities by Activating the Immune Response. Neuron 59 31585809
2011 Drosophila Upf1 and Upf2 loss of function inhibits cell growth and causes animal death in a Upf3-independent manner. RNA (New York, N.Y.) 54 21317294
2015 HIV-1 Recruits UPF1 but Excludes UPF2 to Promote Nucleocytoplasmic Export of the Genomic RNA. Biomolecules 53 26492277
2013 Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2. Nucleic acids research 51 24271394
2016 Human nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complex. Nucleic acids research 46 26740584
2014 UPF2, a nonsense-mediated mRNA decay factor, is required for prepubertal Sertoli cell development and male fertility by ensuring fidelity of the transcriptome. Development (Cambridge, England) 41 25503407
2001 Identification of Cys140 in helix 4 as an exofacial cysteine residue within the substrate-translocation channel of rat equilibrative nitrobenzylthioinosine (NBMPR)-insensitive nucleoside transporter rENT2. The Biochemical journal 41 11139404
2019 UPF2 leads to degradation of dendritically targeted mRNAs to regulate synaptic plasticity and cognitive function. Molecular psychiatry 31 31636381
2018 The RNA surveillance proteins UPF1, UPF2 and SMG6 affect HIV-1 reactivation at a post-transcriptional level. Retrovirology 29 29954456
2006 Upf1/Upf2 regulation of 3' untranslated region splice variants of AUF1 links nonsense-mediated and A+U-rich element-mediated mRNA decay. Molecular and cellular biology 28 17000771
2022 Resistance to ATR Inhibitors Is Mediated by Loss of the Nonsense-Mediated Decay Factor UPF2. Cancer research 24 36273492
2022 Structures of nonsense-mediated mRNA decay factors UPF3B and UPF3A in complex with UPF2 reveal molecular basis for competitive binding and for neurodevelopmental disorder-causing mutation. Nucleic acids research 17 35640974
2022 Modulation of RNA-binding properties of the RNA helicase UPF1 by its activator UPF2. RNA (New York, N.Y.) 17 36456182
2019 Insights into the Effects of Cancer Associated Mutations at the UPF2 and ATP-Binding Sites of NMD Master Regulator: UPF1. International journal of molecular sciences 15 31718065
2024 UPF1 helicase orchestrates mutually exclusive interactions with the SMG6 endonuclease and UPF2. Nucleic acids research 14 38709891
2022 Progression of the pluripotent epiblast depends upon the NMD factor UPF2. Development (Cambridge, England) 14 36255229
2014 A highly conserved region essential for NMD in the Upf2 N-terminal domain. Journal of molecular biology 14 25277656
2002 Role of RNA surveillance proteins Upf1/CpaR, Upf2 and Upf3 in the translational regulation of yeast CPA1 gene. Current genetics 14 12172963
2025 The SARS-CoV-2 nucleocapsid protein interferes with the full enzymatic activation of UPF1 and its interaction with UPF2. Nucleic acids research 7 39831305
2016 Nonsense-mediated mRNA decay factor Upf2 exists in both the nucleoplasm and the cytoplasm. Molecular medicine reports 6 27221324
2013 Proteasome inhibitors and knockdown of SMG1 cause accumulation of Upf1 and Upf2 in human cells. International journal of oncology 6 24173962
2024 Upf2-Mediated Nonsense-Mediated Degradation Pathway Involved in Genetic Compensation of TrpA1 Knockout Mutant Silkworm (Bombyx mori). Insects 5 38786869
2024 In Vitro Cross-Linking MS Reveals SMG1-UPF2-SMG7 Assembly as Molecular Partners within the NMD Surveillance. International journal of molecular sciences 3 38542156
2025 Dynamic RNA binding and unfolding by nonsense-mediated mRNA decay factor UPF2. RNA (New York, N.Y.) 1 40246535
2024 Impact of UPF2 on the levels of CD81 on extracellular vesicles. Frontiers in cell and developmental biology 1 39655046
2023 An alternative spliced UPF2 transcript in pancreatic inflammatory myofibroblastic tumors. Biochemical and biophysical research communications 0 38056247

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