Evidence map›Paper›PMID 31836717›Full record

ArticleNature communications2019

Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4.

Yusuke Sato, Hikaru Tsuchiya, Atsushi Yamagata, Kei Okatsu, Keiji Tanaka, Yasushi Saeki, Shuya Fukai

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

36 citing papers in PubMed, 48 citations in OpenAlex.

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  14. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
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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

7 authors at 4 institutions in 2 countries.

Yusuke SatoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Hikaru TsuchiyaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Atsushi YamagataInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Kei OkatsuInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan. saeki-ys@igakuken.or.jp.ORCID http://orcid.org/0000-0002-9202-5453
Shuya FukaiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan. fukai@iam.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-1241-1443
Tokyo Metropolitan Institute of Medical Science · JPJapan Synchrotron Radiation Research Institute · JPQuantitative BioSciences · USTottori University of Environmental Studies · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Npl4 is likely to be the most upstream factor recognizing Lys48-linked polyubiquitylated substrates in the proteasomal degradation pathway in yeast. Along with Ufd1, Npl4 forms a heterodimer (UN), and functions as a cofactor for the Cdc48 ATPase. Here, we report the crystal structures of yeast Npl4 in complex with Lys48-linked diubiquitin and with the Npl4-binding motif of Ufd1. The distal and proximal ubiquitin moieties of Lys48-linked diubiquitin primarily interact with the C-terminal helix and N-terminal loop of the Npl4 C-terminal domain (CTD), respectively. Mutational analysis suggests that the CTD contributes to linkage selectivity and initial binding of ubiquitin chains. Ufd1 occupies a hydrophobic groove of the Mpr1/Pad1 N-terminal (MPN) domain of Npl4, which corresponds to the catalytic groove of the MPN domain of JAB1/MPN/Mov34 metalloenzyme (JAMM)-family deubiquitylating enzyme. This study provides important structural insights into the polyubiquitin chain recognition by the Cdc48-UN complex and its assembly.

Indexed as

Crystallography, X-RayNucleocytoplasmic Transport ProteinsProteasome Endopeptidase ComplexProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationValosin Containing ProteinVesicular Transport ProteinsCDC48 protein, S cerevisiaeNPL4 protein, S cerevisiaeNucleocytoplasmic Transport ProteinsProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUFD1 protein, S cerevisiaeValosin Containing ProteinVesicular Transport Proteins

Identifiers

PMID31836717
PMCPMC6910952
OpenAlexW2996072429

What OpenQuestion holds

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LicenceCC BY
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.