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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Smg-5 homolog, nonsense mediated mRNA decay factor

SMG5, EST1B, estIb, ever-shorter telomeres 1B, hSMG-5
SMG5 is involved in nonsense-mediated mRNA decay (Ohnishi et al., 2003 [PubMed 14636577]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: caspase-3, UPF1, LIP, SMG, UPF2
Papers on SMG5
A post-translational regulatory switch on UPF1 controls targeted mRNA degradation.
Maquat et al., Rochester, United States. In Genes Dev, 2014
p-UPF1 is enriched on NMD target 3' untranslated regions (UTRs) along with suppressor with morphogenic effect on genitalia 5 (SMG5) and SMG7 but not SMG1 or SMG6.
Phospho-dependent and phospho-independent interactions of the helicase UPF1 with the NMD factors SMG5-SMG7 and SMG6.
Conti et al., Martinsried, Germany. In Nucleic Acids Res, 2014
In human cells, the SMG1 kinase phosphorylates UPF1 at the N-terminal and C-terminal tails, in turn allowing the recruitment of the NMD factors SMG5, SMG6 and SMG7.
The mRNP remodeling mediated by UPF1 promotes rapid degradation of replication-dependent histone mRNA.
Kim et al., Seoul, South Korea. In Nucleic Acids Res, 2014
In addition, hyperphosphorylated UPF1 recruits PNRC2 and SMG5, triggering decapping followed by 5'-to-3' degradation of histone mRNAs.
SMG1 regulates adipogenesis via targeting of staufen1-mediated mRNA decay.
Kim et al., Seoul, South Korea. In Biochim Biophys Acta, 2013
Subsequently, hyperphosphorylated Upf1 associates with SMG5-7 or proline-rich nuclear receptor coregulatory protein (PNRC2) to elicit rapid mRNA degradation.
The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2.
Izaurralde et al., Tübingen, Germany. In Genes Dev, 2013
This degradation is mediated by SMG6, an NMD-specific endonuclease, as well as the SMG5 and SMG7 proteins, which recruit general mRNA decay enzymes.
Yeast hEST1A/B (SMG5/6)-like proteins contribute to environment-sensing adaptive gene expression responses.
Heierhorst et al., Melbourne, Australia. In G3 (bethesda), 2013
Here, we describe two closely related yeast hEST1A-B (SMG5-6)-like proteins termed Esl1 and Esl2 that contain a 14-3-3-like domain and a putative PilT N-terminus ribonuclease domain.
Comparison of EJC-enhanced and EJC-independent NMD in human cells reveals two partially redundant degradation pathways.
Mühlemann et al., In Rna, 2013
Moreover, the relative contributions of both decay pathways differed between the reporters, with PTC-containing immunoglobulin μ transcripts being preferentially subjected to SMG6-mediated endonucleolytic cleavage, whereas β-Globin transcripts were predominantly degraded by the SMG5/SMG7-dependent pathway.
Nonsense-mediated mRNA decay - mechanisms of substrate mRNA recognition and degradation in mammalian cells.
Mühlemann et al., Bern, Switzerland. In Biochim Biophys Acta, 2013
Moreover, we address the role of exon junction complexes (EJCs) in NMD and summarize the functions of SMG5, SMG6 and SMG7 in promoting mRNA decay through different routes.
Role of SMG-1-mediated Upf1 phosphorylation in mammalian nonsense-mediated mRNA decay.
Yamashita, Yokohama, Japan. In Genes Cells, 2013
Phosphorylated-Upf1 recruits the SMG-5/SMG-7 complex to induce ribosome dissociation and decapping-mediated decay.
An unusual arrangement of two 14-3-3-like domains in the SMG5-SMG7 heterodimer is required for efficient nonsense-mediated mRNA decay.
Izaurralde et al., Tübingen, Germany. In Genes Dev, 2013
In metazoans, NMD requires three 14-3-3-like proteins: SMG5, SMG6, and SMG7.
SMG5-PNRC2 is functionally dominant compared with SMG5-SMG7 in mammalian nonsense-mediated mRNA decay.
Kim et al., Seoul, South Korea. In Nucleic Acids Res, 2013
Hyperphosphorylated Upf1 interacts with several factors including SMG5, SMG6, SMG7 and PNRC2 to trigger rapid mRNA degradation.
MARVELD1 Inhibits Nonsense-Mediated RNA Decay by Repressing Serine Phosphorylation of UPF1.
Li et al., Harbin, China. In Plos One, 2012
We also showed that MARVELD1 promotes the dissociation of SMG1 from UPF1, resulting in the repression of serine phosphorylation of UPF1, and subsequently blocks the recruitment of SMG5, which is required for ensuing SMG5-mediated exonucleolytic decay.
Diarrheagenic Escherichia coli detected by 16-plex PCR in raw meat and beef intestines sold at local markets in Ouagadougou, Burkina Faso.
Haukka et al., Helsinki, Finland. In Int J Food Microbiol, 2012
ETEC virulence markers (elt and/or estIb and/or estIa) were detected in 10 (8%) samples and EAEC virulence markers (pic or aggR) in 5 (4%) samples.
Autoregulation of the nonsense-mediated mRNA decay pathway in human cells.
Mühlemann et al., Bern, Switzerland. In Rna, 2011
Using reporter gene assays, we demonstrated that the long 3' UTRs of UPF1, SMG5, and SMG7 mRNAs are the main NMD-inducing features of these mRNAs, suggesting that long 3' UTRs might be a frequent trigger of NMD.
Cutting the nonsense: the degradation of PTC-containing mRNAs.
Mühlemann et al., Bern, Switzerland. In Biochem Soc Trans, 2010
Studies have shown that mammalian NMD targets can be degraded via both an SMG6 (where SMG is suppressor of morphological defects on genitalia)-dependent endonucleolytic pathway and a deadenylation and decapping-dependent exonucleolytic pathway, with the possible involvement of SMG5 and SMG7.
Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation.
Seto et al., Tampa, United States. In Mol Cell Biol, 2006
HDAC8 regulation of hEST1B protein stability modulates total telomerase enzymatic activity
Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7.
Ohno et al., Yokohama, Japan. In Mol Cell, 2003
Data show that phosphorylated hUPF1, the human ortholog of UPF1/SMG-2, forms a complex with human orthologs of the Caenorhabditis elegans proteins SMG-5 and SMG-7.
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