Evidence map›Paper›PMID 27697924›Full record

ArticleThe Journal of cell biology2016

ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation.

Keiji Uematsu, Fumihiko Okumura, Syunsuke Tonogai, Akiko Joo-Okumura, Dawit Hailu Alemayehu, Akihiko Nishikimi, Yoshinori Fukui, Kunio Nakatsukasa, Takumi Kamura

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Keiji UematsuDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Fumihiko OkumuraDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan okumura.fumihiko@a.mbox.nagoya-u.ac.jp z47617a@nucc.cc.nagoya-u.ac.jp.
Syunsuke TonogaiDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Akiko Joo-OkumuraDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Dawit Hailu AlemayehuDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Akihiko NishikimiDivision of Immunogenetics, Department of Immunobiology and Neuroscience, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan Research Center for Advanced Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.ORCID http://orcid.org/0000-0001-9497-7557
Yoshinori FukuiDivision of Immunogenetics, Department of Immunobiology and Neuroscience, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan Research Center for Advanced Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.ORCID http://orcid.org/0000-0003-2335-8745
Kunio NakatsukasaDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Takumi KamuraDivision of Biological Science, Graduate School of Science, Nagoya University, Aichi 464-8602, Japan okumura.fumihiko@a.mbox.nagoya-u.ac.jp z47617a@nucc.cc.nagoya-u.ac.jp.ORCID http://orcid.org/0000-0001-8541-447X
Nagoya University · JPKyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proper dynamic regulation of the spindle is essential for successful cell division. However, the molecular mechanisms that regulate spindle dynamics in mitosis are not fully understood. In this study, we show that Cullin 5-interacting suppressor of cytokine signaling box protein ASB7 ubiquitinates DDA3, a regulator of spindle dynamics, thereby targeting it for proteasomal degradation. The presence of microtubules (MTs) prevented the ASB7-DDA3 interaction, thus stabilizing DDA3. Knockdown of ASB7 decreased MT polymerization and increased the proportion of cells with unaligned chromosomes, and this phenotype was rescued by deletion of DDA3. Collectively, these data indicate that ASB7 plays a crucial role in regulating spindle dynamics and genome integrity by controlling the expression of DDA3.

Indexed as

ProteolysisAnkyrinsCell CycleCell DivisionCullin ProteinsGenome, HumanHEK293 CellsHeLa CellsHumansMicrotubulesModels, BiologicalPhosphoproteinsProteasome Endopeptidase ComplexProtein BindingProtein StabilitySpindle ApparatusAnkyrinsASB7 protein, humanCUL5 protein, humanCullin ProteinsPhosphoproteinsProteasome Endopeptidase ComplexPSRC1 protein, human

Identifiers

PMID27697924
PMCPMC5057283
OpenAlexW2529511684

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.