PubMed:11546873 JSONTXT

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":43,"end":48},"obj":"protein"},{"id":"T2","span":{"begin":419,"end":424},"obj":"protein"},{"id":"T3","span":{"begin":560,"end":565},"obj":"protein"},{"id":"T4","span":{"begin":581,"end":584},"obj":"protein"},{"id":"T5","span":{"begin":655,"end":660},"obj":"protein"},{"id":"T6","span":{"begin":676,"end":679},"obj":"protein"},{"id":"T7","span":{"begin":731,"end":738},"obj":"protein"},{"id":"T8","span":{"begin":743,"end":746},"obj":"protein"},{"id":"T9","span":{"begin":780,"end":785},"obj":"protein"},{"id":"T10","span":{"begin":803,"end":808},"obj":"protein"},{"id":"T11","span":{"begin":871,"end":874},"obj":"protein"},{"id":"T12","span":{"begin":879,"end":886},"obj":"protein"},{"id":"T13","span":{"begin":888,"end":893},"obj":"protein"},{"id":"T14","span":{"begin":1029,"end":1034},"obj":"protein"}],"text":"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.\nNonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically ( approximately 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm."}

{"project":"PIR-corpus2","denotations":[{"id":"T1","span":{"begin":12,"end":48},"obj":"protein"},{"id":"T2","span":{"begin":419,"end":424},"obj":"protein"},{"id":"T3","span":{"begin":435,"end":450},"obj":"protein"},{"id":"T4","span":{"begin":560,"end":565},"obj":"protein"},{"id":"T5","span":{"begin":588,"end":600},"obj":"protein"},{"id":"T6","span":{"begin":655,"end":660},"obj":"protein"},{"id":"T7","span":{"begin":676,"end":705},"obj":"protein"},{"id":"T8","span":{"begin":711,"end":738},"obj":"protein"},{"id":"T9","span":{"begin":743,"end":746},"obj":"protein"},{"id":"T10","span":{"begin":772,"end":785},"obj":"protein"},{"id":"T11","span":{"begin":803,"end":808},"obj":"protein"},{"id":"T12","span":{"begin":815,"end":819},"obj":"protein"},{"id":"T13","span":{"begin":879,"end":886},"obj":"protein"},{"id":"T14","span":{"begin":888,"end":893},"obj":"protein"},{"id":"T15","span":{"begin":1029,"end":1034},"obj":"protein"}],"text":"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.\nNonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically ( approximately 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm."}

{"project":"PIR-corpus1","denotations":[{"id":"T1","span":{"begin":43,"end":48},"obj":"protein"},{"id":"T2","span":{"begin":419,"end":424},"obj":"protein"},{"id":"T3","span":{"begin":443,"end":450},"obj":"protein"},{"id":"T4","span":{"begin":560,"end":565},"obj":"protein"},{"id":"T5","span":{"begin":581,"end":584},"obj":"protein"},{"id":"T6","span":{"begin":588,"end":600},"obj":"protein"},{"id":"T7","span":{"begin":655,"end":660},"obj":"protein"},{"id":"T8","span":{"begin":691,"end":705},"obj":"protein"},{"id":"T9","span":{"begin":716,"end":738},"obj":"protein"},{"id":"T10","span":{"begin":780,"end":785},"obj":"protein"},{"id":"T11","span":{"begin":803,"end":808},"obj":"protein"},{"id":"T12","span":{"begin":815,"end":819},"obj":"protein"},{"id":"T13","span":{"begin":871,"end":874},"obj":"protein"},{"id":"T14","span":{"begin":879,"end":886},"obj":"protein"},{"id":"T15","span":{"begin":888,"end":893},"obj":"protein"},{"id":"T16","span":{"begin":1029,"end":1034},"obj":"protein"},{"id":"T17","span":{"begin":1074,"end":1081},"obj":"protein"}],"text":"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.\nNonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically ( approximately 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm."}