SMG6 Antibody

1. Nonsense-mediated mRNA decay (NMD) substrates with PTCs undergo constitutive SMG6-dependent endocleavage, rather than SMG7-dependent exonucleolytic decay. In contrast, the turnover of NMD substrates containing upstream ORFs and long 3' UTRs involves both SMG6- and SMG7-dependent endo- and exonucleolytic decay, respectively; extent to which SMG6 and SMG7 degrade NMD substrates is determined by the mRNA architecture. PMID: 28461625
2. Transcriptome-wide identification of nonsense-mediated mRNA decay-targeted human mRNAs reveals extensive redundancy between SMG6- and SMG7-mediated degradation pathways. PMID: 27864472
3. A preferred sequence motif spanning most SMG6 cleavage sites has been discovered by analysis of endogenous non-sense-mediated mRNA decay targets. PMID: 25429978
4. SMG6 requires UPF1 and SMG1 for nonsense-mediated mRNA decay. PMID: 25053839
5. The study demonstrates that SMG5-SMG7 and SMG6 exhibit different and non-overlapping modes of UPF1 recognition, thus pointing at distinguished roles in integrating the complex nonsense-mediated mRNA decay interaction network. PMID: 25013172
6. Consistent with involvement of SMG6 in the decay process full-length nonsense-containing beta-globin mRNA was increased and the Delta169 decay intermediate was decreased in cells knocked down for SMG6. PMID: 24086375
7. The tricotetrapeptide repeat-containing domain within Est1A was sufficient for interaction with hTERT. PMID: 22011238
8. Data show that SMG6 interacts directly with the EJC via two conserved EJC-binding motifs (EBMs). PMID: 20930030
9. associated with most or all active telomerase in HeLa cell extracts; overexpression of hEST1A induces anaphase bridges due to chromosome-end fusions, and telomeric DNA persists at the fusion points PMID: 12676087
10. Human EST1A is associated with most or all active telomerase and is involved either directly or indirectly in telomere elongation and telomere capping. PMID: 16820686
11. Structural properties of the PIN domain indicate its putative active center consisting of invariant acidic amino acid residues, which is similar to the active center of 5' nucleases. PMID: 17557331
12. Report shows that hEST1A assembles specifically with telomerase in the context of the telomerase RNA (hTR)-hTERT ribonucleoprotein, through the high affinity of hEST1A for hTR and specific protein-protein contacts with hTERT. PMID: 17940095

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HGNC: 17809

OMIM: 610963

KEGG: hsa:23293

STRING: 9606.ENSP00000263073

UniGene: Hs.448342