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  Human nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complex

Lopez-Perrote, A., Castano, R., Melero, R., Zamarro, T., Kurosawa, H., Ohnishi, T., et al. (2016). Human nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complex. NUCLEIC ACIDS RESEARCH, 44(4), 1909-1923. doi:10.1093/nar/gkv1527.

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 Creators:
Lopez-Perrote, Andres1, Author
Castano, Raquel1, Author
Melero, Roberto1, Author
Zamarro, Teresa1, Author
Kurosawa, Hitomi1, Author
Ohnishi, Tetsuo1, Author
Uchiyama, Akiko1, Author
Aoyagi, Kyoko1, Author
Buchwald, Gretel2, Author              
Kataoka, Naoyuki1, Author
Yamashita, Akio1, Author
Llorca, Oscar1, Author
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1external, ou_persistent22              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: EXON JUNCTION COMPLEX; CRYO-EM STRUCTURE; STEM-CELL DIFFERENTIATION; TERMINATION COMPLEX; ELECTRON-MICROSCOPY; TRANSLATION TERMINATION; SURVEILLANCE COMPLEX; STRUCTURAL INSIGHTS; FUNCTIONAL-ANALYSIS; CRYSTAL-STRUCTURE
 Abstract: Nonsense-mediated mRNA decay (NMD) is an mRNA degradation pathway that regulates gene expression and mRNA quality. A complex network of macromolecular interactions regulates NMD initiation, which is only partially understood. According to prevailing models, NMD begins by the assembly of the SURF (SMG1-UPF1-eRF1-eRF3) complex at the ribosome, followed by UPF1 activation by additional factors such as UPF2 and UPF3. Elucidating the interactions between NMD factors is essential to comprehend NMD, and here we demonstrate biochemically and structurally the interaction between human UPF2 and eukaryotic release factor 3 (eRF3). In addition, we find that UPF2 associates with SURF and ribosomes in cells, in an UPF3-independent manner. Binding assays using a collection of UPF2 truncated variants reveal that eRF3 binds to the C-terminal part of UPF2. This region of UPF2 is partially coincident with the UPF3-binding site as revealed by electron microscopy of the UPF2-eRF3 complex. Accordingly, we find that the interaction of UPF2 with UPF3b interferes with the assembly of the UPF2-eRF3 complex, and that UPF2 binds UPF3b more strongly than eRF3. Together, our results highlight the role of UPF2 as a platform for the transient interactions of several NMD factors, including several components of SURF.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000371519700044
DOI: 10.1093/nar/gkv1527
 Degree: -

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Title: NUCLEIC ACIDS RESEARCH
Source Genre: Journal
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Publ. Info: GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND : OXFORD UNIV PRESS
Pages: - Volume / Issue: 44 (4) Sequence Number: - Start / End Page: 1909 - 1923 Identifier: ISSN: 0305-1048