Evidence map›Paper›PMID 25635053›Full record

ArticleThe Journal of biological chemistry2015

Disrupted-in-schizophrenia 1 (DISC1) regulates dysbindin function by enhancing its stability.

Seol-Ae Lee, Seong-Mo Kim, Bo Kyoung Suh, Hwa-Young Sun, Young-Un Park, Ji-Ho Hong, Cana Park, Minh Dang Nguyen, Koh-Ichi Nagata, Joo-Yeon Yoo and 1 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Dysbindin-1 Involvement in the Etiology of Schizophrenia.International journal of molecular sciences · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. RNA Sequencing in Schizophrenia.Bioinformatics and biology insights · 2015
    Review
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

11 authors.

Seol-Ae LeeFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Seong-Mo KimFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Bo Kyoung SuhFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Hwa-Young SunFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Young-Un ParkFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Ji-Ho HongFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Cana ParkFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Minh Dang Nguyenthe Hotchkiss Brain Institute, Departments of Clinical Neurosciences, Cell Biology and Anatomy, and Biochemistry and Molecular Biology, University of Calgary, Calgary T2N 4N1, Canada, and.
Koh-Ichi Nagatathe Department of Molecular Neurobiology, Institute for Developmental Research, Aichi Human Service Center, 713-8 Kamiya, Kasugai 480-0392, Japan.
Joo-Yeon YooFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Sang Ki ParkFrom the Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea, skpark@postech.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysbindin and DISC1 are schizophrenia susceptibility factors playing roles in neuronal development. Here we show that the physical interaction between dysbindin and DISC1 is critical for the stability of dysbindin and for the process of neurite outgrowth. We found that DISC1 forms a complex with dysbindin and increases its stability in association with a reduction in ubiquitylation. Furthermore, knockdown of DISC1 or expression of a deletion mutant, DISC1 lacking amino acid residues 403-504 of DISC1 (DISC1(Δ403-504)), effectively decreased levels of endogenous dysbindin. Finally, the neurite outgrowth defect induced by knockdown of DISC1 was partially reversed by coexpression of dysbindin. Taken together, these results indicate that dysbindin and DISC1 form a physiologically functional complex that is essential for normal neurite outgrowth.

Indexed as

AnimalsCells, CulturedCerebral CortexChlorocebus aethiopsCOS CellsDysbindinDystrophin-Associated ProteinsHEK293 CellsHumansMiceNerve Tissue ProteinsNeuritesNeuronsProteasome Endopeptidase ComplexProtein StabilityUbiquitinDISC1 protein, humanDisc1 protein, mouseDTNBP1 protein, humanDtnbp1 protein, mouseDysbindinDystrophin-Associated ProteinsNerve Tissue ProteinsProteasome Endopeptidase ComplexUbiquitinDISC1DysbindinNeurite OutgrowthProtein ComplexProtein StabilitySchizophreniaUbiquitylation (Ubiquitination)

Identifiers

PMID25635053
PMCPMC4358130

What OpenQuestion holds

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Registered trials

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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.