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SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway

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SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway. / Fukuhara, Noemi; Ebert, Judith; Unterholzner, Leonie et al.
In: Molecular Cell, Vol. 17, No. 4, 18.02.2005, p. 537-547.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Fukuhara, N, Ebert, J, Unterholzner, L, Lindner, D, Izaurralde, E & Conti, E 2005, 'SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway', Molecular Cell, vol. 17, no. 4, pp. 537-547. https://doi.org/10.1016/j.molcel.2005.01.010

APA

Fukuhara, N., Ebert, J., Unterholzner, L., Lindner, D., Izaurralde, E., & Conti, E. (2005). SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway. Molecular Cell, 17(4), 537-547. https://doi.org/10.1016/j.molcel.2005.01.010

Vancouver

Fukuhara N, Ebert J, Unterholzner L, Lindner D, Izaurralde E, Conti E. SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway. Molecular Cell. 2005 Feb 18;17(4):537-547. Epub 2005 Feb 17. doi: 10.1016/j.molcel.2005.01.010

Author

Fukuhara, Noemi ; Ebert, Judith ; Unterholzner, Leonie et al. / SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway. In: Molecular Cell. 2005 ; Vol. 17, No. 4. pp. 537-547.

Bibtex

@article{e2e024c2c27240f5bcea55fe5a5fe9cf,
title = "SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway",
abstract = "In metazoa, regulation of the phosphorylation state of UPF1 is crucial for nonsense-mediated mRNA decay (NMD), a process by which aberrant mRNAs containing nonsense mutations are degraded. UPF1 is targeted for dephosphorylation by three related proteins, SMG5, SMG6, and SMG7. We report here the crystal structure of the N-terminal domain of SMG7. The structure reveals that SMG7 contains a 14-3-3-like domain. Residues that bind phosphoserine-containing peptides in 14-3-3 are conserved at the equivalent positions in SMG7. Mutation of these residues impairs UPF1 binding to SMG7 in vitro and UPF1 recruitment to cytoplasmic mRNA decay foci in vivo, suggesting that SMG7 acts as an adaptor in targeting mRNAs associated with phosphorylated UPF1 for degradation. The 14-3-3 site of SMG7 is conserved in SMG5 and SMG6. These data also imply that the homologous human Est1 might have a 14-3-3 function at telomeres, and that phosphorylation events may be important for telomerase regulation.",
keywords = "14-3-3 Proteins, Amino Acid Sequence, Carrier Proteins, Codon, Nonsense, Cytoplasm, HeLa Cells, Humans, Molecular Sequence Data, Mutation, Peptide Fragments, Phosphorylation, Phosphoserine, Protein Conformation, Protein Folding, Protein Structure, Tertiary, RNA Stability, RNA, Messenger, Sequence Homology, Amino Acid, Signal Transduction",
author = "Noemi Fukuhara and Judith Ebert and Leonie Unterholzner and Doris Lindner and Elisa Izaurralde and Elena Conti",
year = "2005",
month = feb,
day = "18",
doi = "10.1016/j.molcel.2005.01.010",
language = "English",
volume = "17",
pages = "537--547",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway

AU - Fukuhara, Noemi

AU - Ebert, Judith

AU - Unterholzner, Leonie

AU - Lindner, Doris

AU - Izaurralde, Elisa

AU - Conti, Elena

PY - 2005/2/18

Y1 - 2005/2/18

N2 - In metazoa, regulation of the phosphorylation state of UPF1 is crucial for nonsense-mediated mRNA decay (NMD), a process by which aberrant mRNAs containing nonsense mutations are degraded. UPF1 is targeted for dephosphorylation by three related proteins, SMG5, SMG6, and SMG7. We report here the crystal structure of the N-terminal domain of SMG7. The structure reveals that SMG7 contains a 14-3-3-like domain. Residues that bind phosphoserine-containing peptides in 14-3-3 are conserved at the equivalent positions in SMG7. Mutation of these residues impairs UPF1 binding to SMG7 in vitro and UPF1 recruitment to cytoplasmic mRNA decay foci in vivo, suggesting that SMG7 acts as an adaptor in targeting mRNAs associated with phosphorylated UPF1 for degradation. The 14-3-3 site of SMG7 is conserved in SMG5 and SMG6. These data also imply that the homologous human Est1 might have a 14-3-3 function at telomeres, and that phosphorylation events may be important for telomerase regulation.

AB - In metazoa, regulation of the phosphorylation state of UPF1 is crucial for nonsense-mediated mRNA decay (NMD), a process by which aberrant mRNAs containing nonsense mutations are degraded. UPF1 is targeted for dephosphorylation by three related proteins, SMG5, SMG6, and SMG7. We report here the crystal structure of the N-terminal domain of SMG7. The structure reveals that SMG7 contains a 14-3-3-like domain. Residues that bind phosphoserine-containing peptides in 14-3-3 are conserved at the equivalent positions in SMG7. Mutation of these residues impairs UPF1 binding to SMG7 in vitro and UPF1 recruitment to cytoplasmic mRNA decay foci in vivo, suggesting that SMG7 acts as an adaptor in targeting mRNAs associated with phosphorylated UPF1 for degradation. The 14-3-3 site of SMG7 is conserved in SMG5 and SMG6. These data also imply that the homologous human Est1 might have a 14-3-3 function at telomeres, and that phosphorylation events may be important for telomerase regulation.

KW - 14-3-3 Proteins

KW - Amino Acid Sequence

KW - Carrier Proteins

KW - Codon, Nonsense

KW - Cytoplasm

KW - HeLa Cells

KW - Humans

KW - Molecular Sequence Data

KW - Mutation

KW - Peptide Fragments

KW - Phosphorylation

KW - Phosphoserine

KW - Protein Conformation

KW - Protein Folding

KW - Protein Structure, Tertiary

KW - RNA Stability

KW - RNA, Messenger

KW - Sequence Homology, Amino Acid

KW - Signal Transduction

U2 - 10.1016/j.molcel.2005.01.010

DO - 10.1016/j.molcel.2005.01.010

M3 - Journal article

C2 - 15721257

VL - 17

SP - 537

EP - 547

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -