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SMG7 acts as a molecular link between mRNA surveillance and mRNA decay

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SMG7 acts as a molecular link between mRNA surveillance and mRNA decay. / Unterholzner, Leonie; Izaurralde, Elisa.
In: Molecular Cell, Vol. 16, No. 4, 19.11.2004, p. 587-596.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

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Unterholzner L, Izaurralde E. SMG7 acts as a molecular link between mRNA surveillance and mRNA decay. Molecular Cell. 2004 Nov 19;16(4):587-596. Epub 2004 Nov 18. doi: 10.1016/j.molcel.2004.10.013

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Unterholzner, Leonie ; Izaurralde, Elisa. / SMG7 acts as a molecular link between mRNA surveillance and mRNA decay. In: Molecular Cell. 2004 ; Vol. 16, No. 4. pp. 587-596.

Bibtex

@article{67b981462bbd44ecb07230c69627d684,
title = "SMG7 acts as a molecular link between mRNA surveillance and mRNA decay",
abstract = "Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism that eliminates mRNAs containing premature termination codons (PTCs). The proteins UPF1, SMG5, SMG6, and SMG7 are essential NMD factors in metazoa. SMG5 and SMG7 form a complex with UPF1 and interact with each other via their N-terminal domains. Here we show that SMG5 and SMG7 colocalize in cytoplasmic mRNA decay bodies, while SMG6 forms separate cytoplasmic foci. When SMG7 is tethered to a reporter transcript, it elicits its degradation, bypassing the requirement for a PTC, UPF1, SMG5, or SMG6. This activity is mediated by the C-terminal domain of SMG7. In contrast, SMG5 requires SMG7 to trigger mRNA decay and to localize to decay bodies. Our findings indicate that SMG7 provides a link between the NMD and the mRNA degradation machinery by interacting with SMG5 and UPF1 via its N-terminal domain and targeting bound transcripts for decay via its C-terminal domain.",
keywords = "Blotting, Western, Carbocyanines, Carrier Proteins, Cytoplasm, Dactinomycin, Frameshift Mutation, Genes, Reporter, HeLa Cells, Humans, Luciferases, Microscopy, Fluorescence, Mutation, Nucleic Acid Synthesis Inhibitors, Plasmids, Protein Structure, Tertiary, RNA Interference, RNA, Messenger, RNA, Small Interfering, Recombinant Fusion Proteins, Ribonucleoproteins, Small Nuclear, Templates, Genetic, Time Factors, Trans-Activators, Transfection",
author = "Leonie Unterholzner and Elisa Izaurralde",
year = "2004",
month = nov,
day = "19",
doi = "10.1016/j.molcel.2004.10.013",
language = "English",
volume = "16",
pages = "587--596",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - SMG7 acts as a molecular link between mRNA surveillance and mRNA decay

AU - Unterholzner, Leonie

AU - Izaurralde, Elisa

PY - 2004/11/19

Y1 - 2004/11/19

N2 - Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism that eliminates mRNAs containing premature termination codons (PTCs). The proteins UPF1, SMG5, SMG6, and SMG7 are essential NMD factors in metazoa. SMG5 and SMG7 form a complex with UPF1 and interact with each other via their N-terminal domains. Here we show that SMG5 and SMG7 colocalize in cytoplasmic mRNA decay bodies, while SMG6 forms separate cytoplasmic foci. When SMG7 is tethered to a reporter transcript, it elicits its degradation, bypassing the requirement for a PTC, UPF1, SMG5, or SMG6. This activity is mediated by the C-terminal domain of SMG7. In contrast, SMG5 requires SMG7 to trigger mRNA decay and to localize to decay bodies. Our findings indicate that SMG7 provides a link between the NMD and the mRNA degradation machinery by interacting with SMG5 and UPF1 via its N-terminal domain and targeting bound transcripts for decay via its C-terminal domain.

AB - Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism that eliminates mRNAs containing premature termination codons (PTCs). The proteins UPF1, SMG5, SMG6, and SMG7 are essential NMD factors in metazoa. SMG5 and SMG7 form a complex with UPF1 and interact with each other via their N-terminal domains. Here we show that SMG5 and SMG7 colocalize in cytoplasmic mRNA decay bodies, while SMG6 forms separate cytoplasmic foci. When SMG7 is tethered to a reporter transcript, it elicits its degradation, bypassing the requirement for a PTC, UPF1, SMG5, or SMG6. This activity is mediated by the C-terminal domain of SMG7. In contrast, SMG5 requires SMG7 to trigger mRNA decay and to localize to decay bodies. Our findings indicate that SMG7 provides a link between the NMD and the mRNA degradation machinery by interacting with SMG5 and UPF1 via its N-terminal domain and targeting bound transcripts for decay via its C-terminal domain.

KW - Blotting, Western

KW - Carbocyanines

KW - Carrier Proteins

KW - Cytoplasm

KW - Dactinomycin

KW - Frameshift Mutation

KW - Genes, Reporter

KW - HeLa Cells

KW - Humans

KW - Luciferases

KW - Microscopy, Fluorescence

KW - Mutation

KW - Nucleic Acid Synthesis Inhibitors

KW - Plasmids

KW - Protein Structure, Tertiary

KW - RNA Interference

KW - RNA, Messenger

KW - RNA, Small Interfering

KW - Recombinant Fusion Proteins

KW - Ribonucleoproteins, Small Nuclear

KW - Templates, Genetic

KW - Time Factors

KW - Trans-Activators

KW - Transfection

U2 - 10.1016/j.molcel.2004.10.013

DO - 10.1016/j.molcel.2004.10.013

M3 - Journal article

C2 - 15546618

VL - 16

SP - 587

EP - 596

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -