Evidence map›Paper›PMID 29666234›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Nuclear export of ubiquitinated proteins via the UBIN-POST system.

Shoshiro Hirayama, Munechika Sugihara, Daisuke Morito, Shun-Ichiro Iemura, Tohru Natsume, Shigeo Murata, Kazuhiro Nagata

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

25 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
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  4. Article
  5. Article
  6. Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025
    Review
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  13. iScience · 2023
    Article
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  19. Article
  20. Nuclear envelope budding is a response to cellular stress.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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.

Shoshiro HirayamaLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, 113-0033, Japan; s.hirayama@mol.f.u-tokyo.ac.jp nagata@cc.kyoto-su.ac.jp.ORCID 0000-0002-5141-8461
Munechika SugiharaFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8555, Japan.
Daisuke MoritoInstitute for Protein Dynamics, Kyoto Sangyo University, Kyoto, 603-8555, Japan.
Shun-Ichiro IemuraBiomedicinal Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, 135-0064, Japan.
Tohru NatsumeBiomedicinal Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, 135-0064, Japan.
Shigeo MurataLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, 113-0033, Japan.ORCID 0000-0002-3177-3503
Kazuhiro NagataFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8555, Japan; s.hirayama@mol.f.u-tokyo.ac.jp nagata@cc.kyoto-su.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although mechanisms for protein homeostasis in the cytosol have been studied extensively, those in the nucleus remain largely unknown. Here, we identified that a protein complex mediates export of polyubiquitinated proteins from the nucleus to the cytosol. UBIN, a ubiquitin-associated (UBA) domain-containing protein, shuttled between the nucleus and the cytosol in a CRM1-dependent manner, despite the lack of intrinsic nuclear export signal (NES). Instead, the UBIN binding protein polyubiquitinated substrate transporter (POST) harboring an NES shuttled UBIN through nuclear pores. UBIN bound to polyubiquitin chain through its UBA domain, and the UBIN-POST complex exported them from the nucleus to the cytosol. Ubiquitinated proteins accumulated in the cytosol in response to proteasome inhibition, whereas cotreatment with CRM1 inhibitor led to their accumulation in the nucleus. Our results suggest that ubiquitinated proteins are exported from the nucleus to the cytosol in the UBIN-POST complex-dependent manner for the maintenance of nuclear protein homeostasis.

Indexed as

Active Transport, Cell NucleusAnimalsCarrier ProteinsCell NucleusCytosolHEK293 CellsHeLa CellsHumansHuman Umbilical Vein Endothelial CellsMembrane ProteinsMiceNIH 3T3 CellsNuclear ProteinsSolute Carrier ProteinsUbiquitinated ProteinsCarrier ProteinsMembrane ProteinsNuclear ProteinsSLC35G1 protein, humanSolute Carrier ProteinsUbiquitinated ProteinsUBQLN4 protein, humanprotein aggregationprotein quality controlprotein transportubiquitin

Identifiers

PMID29666234
PMCPMC5939056

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.