Evidence map›Paper›PMID 21965535›Full record

ArticleNucleic acids research2012

N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD.

Yukiko Okada-Katsuhata, Akio Yamashita, Kei Kutsuzawa, Natsuko Izumi, Fumiki Hirahara, Shigeo Ohno

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
8.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

160 citing papers in PubMed, 257 citations in OpenAlex.

  1. Article
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    Review
  3. NMD takes two PIN domains to tango.RNA (New York, N.Y.) · 2026
    Article
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  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

100 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Yukiko Okada-KatsuhataDepartment of Molecular Biology, Yokohama City University, School of Medicine, 3-9, Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan.
Akio Yamashita
Kei Kutsuzawa
Natsuko Izumi
Fumiki Hirahara
Shigeo Ohno
Japan Science and Technology Agency · JPYokohama City University · JPYokohama City University Medical Center · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism that detects and degrades mRNAs containing premature termination codons (PTCs). SMG-1-mediated Upf1 phosphorylation takes place in the decay inducing complex (DECID), which contains a ribosome, release factors, Upf1, SMG-1, an exon junction complex (EJC) and a PTC-mRNA. However, the significance and the consequence of Upf1 phosphorylation remain to be clarified. Here, we demonstrate that SMG-6 binds to a newly identified phosphorylation site in Upf1 at N-terminal threonine 28, whereas the SMG-5:SMG-7 complex binds to phosphorylated serine 1096 of Upf1. In addition, the binding of the SMG-5:SMG-7 complex to Upf1 resulted in the dissociation of the ribosome and release factors from the DECID complex. Importantly, the simultaneous binding of both the SMG-5:SMG-7 complex and SMG-6 to phospho-Upf1 are required for both NMD and Upf1 dissociation from mRNA. Thus, the SMG-1-mediated phosphorylation of Upf1 creates a binding platforms for the SMG-5:SMG-7 complex and for SMG-6, and triggers sequential remodeling of the mRNA surveillance complex for NMD induction and recycling of the ribosome, release factors and NMD factors.

Indexed as

Nonsense Mediated mRNA Decay14-3-3 ProteinsBinding SitesCarrier ProteinsEndoribonucleasesHEK293 CellsHeLa CellsHumansPhosphatidylinositol 3-KinasesPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryRNA HelicasesTelomeraseThreonineTrans-Activators14-3-3 ProteinsCarrier ProteinsEndoribonucleasesPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesRNA HelicasesSMG1 protein, humanSMG5 protein, humanSMG6 protein, humanSMG7 protein, humanTelomeraseThreonineTrans-ActivatorsUPF1 protein, human

Identifiers

PMID21965535
PMCPMC3273798
OpenAlexW2052815918

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.