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UPF2 regulator of nonsense transcripts homolog

UPF2, hUpf2, NMD2, Nmd2p
This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein is located in the perinuclear area. It interacts with translation release factors and the proteins that are functional homologs of yeast Upf1p and Upf3p. Two splice variants have been found for this gene; both variants encode the same protein. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: caspase-3, UPF1, UPF3, CAN, LIP
Papers on UPF2
Human nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complex.
Llorca et al., Madrid, Spain. In Nucleic Acids Res, Feb 2016
According to prevailing models, NMD begins by the assembly of the SURF (SMG1-UPF1-eRF1-eRF3) complex at the ribosome, followed by UPF1 activation by additional factors such as UPF2 and UPF3.
Caspases shutdown nonsense-mediated mRNA decay during apoptosis.
Lejeune et al., Lille, France. In Cell Death Differ, Nov 2015
The present study shows that caspases cleave the two NMD factors UPF1 and UPF2 during apoptosis impairing NMD.
Intranuclear binding in space and time of exon junction complex and NXF1 to premRNPs/mRNPs in vivo.
Wieslander et al., Stockholm, Sweden. In J Cell Biol, Nov 2015
The EJC core does not recruit the nonsense-mediated decay mediaters UPF2 and UPF3 until the BR messenger RNA protein complexes (mRNPs) enter the interchromatin.
A network of SMG-8, SMG-9 and SMG-1 C-terminal insertion domain regulates UPF1 substrate recruitment and phosphorylation.
Schaffitzel et al., Grenoble, France. In Nucleic Acids Res, Oct 2015
The presence of UPF2 destabilizes the SMG-1-8-9-UPF1 complex leading to substrate release.
Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1.
Finkbeiner et al., San Francisco, United States. In Proc Natl Acad Sci U S A, Jul 2015
Expression of hUPF2, another essential component of NMD, also improves survival, whereas inhibiting NMD prevents rescue by hUPF1, suggesting that hUPF1 acts through NMD to enhance survival.
UPF2, a nonsense-mediated mRNA decay factor, is required for prepubertal Sertoli cell development and male fertility by ensuring fidelity of the transcriptome.
Yan et al., Reno, United States. In Development, Feb 2015
Here, we report that ablation of Upf2, which encodes a core NMD factor, in murine embryonic Sertoli cells (SCs) leads to severe testicular atrophy and male sterility owing to rapid depletion of both SCs and germ cells during prepubertal testicular development.
HIV-1 Recruits UPF1 but Excludes UPF2 to Promote Nucleocytoplasmic Export of the Genomic RNA.
Mouland et al., Montréal, Canada. In Biomolecules, 2014
Interestingly, we observed that both UPF2 and the long isoform of UPF3a, UPF3aL, but not the shorter isoforms UPF3aS and UPF3b, are excluded from the UPF1-Rev-CRM1-DDX3 complex as they are negative regulators of vRNA nuclear export.
3' UTR length and messenger ribonucleoprotein composition determine endocleavage efficiencies at termination codons.
Gehring et al., Köln, Germany. In Cell Rep, 2014
Whereas the core NMD component UPF2 supports endonucleolytic decay of long 3' UTR mRNAs, it is mostly dispensable during EJC-stimulated endocleavage.
The RNA helicase DHX34 activates NMD by promoting a transition from the surveillance to the decay-inducing complex.
Cáceres et al., Edinburgh, United Kingdom. In Cell Rep, 2014
Subsequently, an interaction with UPF2, UPF3b, and the exon junction complex induces the formation of the decay-inducing complex (DECID) and triggers NMD.
Juggling key players in NMD initiation.
Bono, Tübingen, Germany. In Structure, 2014
In this issue of Structure, Melero and colleagues use electron microscopy combined with biochemistry to provide structural insight into the complex between SMG1, SMG8, SMG9, UPF1, and UPF2, elucidating how key players in nonsense-mediated mRNA decay assemble at the initial steps of the process.
Control of somatic tissue differentiation by the long non-coding RNA TINCR.
Khavari et al., Stanford, United States. In Nature, 2013
Loss of UPF1 and UPF2, both of which are required for STAU1-mediated RNA decay, however, did not have differentiation effects.
Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2.
Conti et al., Martinsried, Germany. In Mol Cell, 2011
Data show that upon binding to Upf2, the regulatory CH domain of Upf1 undergoes a large conformational change, causing the catalytic helicase domain to bind RNA less extensively and triggering its helicase activity.
UPF2 is a critical regulator of liver development, function and regeneration.
Porse et al., Copenhagen, Denmark. In Plos One, 2009
Study find that loss of Upf2 during fetal liver development is incompatible with postnatal life due to failure of terminal differentiation. Moreover, deletion of Upf2 in the adult liver results in hepatosteatosis and disruption of liver homeostasis.
Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2.
Cusack et al., Grenoble, France. In Embo J, 2009
The authors propose that the bipartite mode of UPF2 binding to UPF1 brings the ribosome and the exon junction complex in close proximity by forming a tight complex after an initial weak encounter with either element.
UPF1 P-body localization.
Wen et al., Birmingham, United Kingdom. In Biochem Soc Trans, 2008
However, recent studies have indicated that the core NMD factors UPF1 (up-frameshift-1), UPF2 and UPF3 can associate with P-bodies (processing bodies), which are large cytoplasmic granules replete with proteins involved in general mRNA decay and related processes.
NMD is essential for hematopoietic stem and progenitor cells and for eliminating by-products of programmed DNA rearrangements.
Porse et al., Copenhagen, Denmark. In Genes Dev, 2008
Hematopoietic-specific deletion of Upf2, a core NMD factor, led to the rapid, complete, and lasting cell-autonomous extinction of all hematopoietic stem and progenitor populations.
NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity.
Le Hir et al., Gif-sur-Yvette, France. In Nat Struct Mol Biol, 2008
UPF2 and UPF3b cooperatively stimulate both ATPase and RNA helicase activities of UPF1.
A new function for nonsense-mediated mRNA-decay factors.
Wilkinson, Houston, United States. In Trends Genet, 2005
Surprisingly, recent evidence strongly suggests that the NMD factors UPF1, UPF2, UPF3B, RNPS1, Y14 and MAGOH also promote translation of normal mRNAs in mammalian cells.
Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts.
Dietz et al., Baltimore, United States. In Science, 2002
In contrast, inhibition of rent2/hUpf2 expression did not disrupt NAS despite achieving comparable stabilization of nonsense transcripts.
Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon.
Steitz et al., New Haven, United States. In Cell, 2001
We describe three novel human proteins involved in NMD, hUpf2, hUpf3a, and hUpf3b.
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