Evidence map›Paper›PMID 19696028›Full record

ArticleThe Journal of biological chemistry2009

Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases.

Reiko Ban, Hideki Matsuzaki, Tomohiro Akashi, Gyosuke Sakashita, Hisaaki Taniguchi, Sam-Yong Park, Hirofumi Tanaka, Koichi Furukawa, Takeshi Urano

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 49 citations in OpenAlex.

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  14. Microtubule plus-end tracking proteins in neuronal development.Cellular and molecular life sciences : CMLS · 2016
    Review
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  20. Regulators and effectors of Siah ubiquitin ligases.Cell biochemistry and biophysics · 2013
    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

9 authors at 5 institutions in 1 country.

Reiko BanDepartment of Biochemistry, Shimane University School of Medicine, Izumo 693-8501; Department of Biochemistry, Nagoya University Graduate School of Medicine, Nagoya 466-8550. Electronic address: banrei@med.shimane-u.ac.jp.
Hideki MatsuzakiInstitute for Enzyme Research, University of Tokushima, 3-15-18 Kuramoto, Tokushima 770-8503.
Tomohiro AkashiDivision of Molecular Mycology and Medicine, Nagoya University Graduate School of Medicine, Nagoya 466-8550.
Gyosuke SakashitaDepartment of Biochemistry, Shimane University School of Medicine, Izumo 693-8501; Department of Biochemistry, Nagoya University Graduate School of Medicine, Nagoya 466-8550.
Hisaaki TaniguchiInstitute for Enzyme Research, University of Tokushima, 3-15-18 Kuramoto, Tokushima 770-8503.
Sam-Yong ParkProtein Design Laboratory, Yokohama City University, Tsurumi, Yokohama 230-0045.
Hirofumi TanakaSchool of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan.
Koichi FurukawaDepartment of Biochemistry, Nagoya University Graduate School of Medicine, Nagoya 466-8550.
Takeshi UranoDepartment of Biochemistry, Shimane University School of Medicine, Izumo 693-8501; Department of Biochemistry, Nagoya University Graduate School of Medicine, Nagoya 466-8550. Electronic address: turano@med.shimane-u.ac.jp.
Nagoya University · JPTokushima University · JPShimane University · JPThe University of Tokyo · JPYokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule plus-end tracking proteins (+TIPs) control microtubule dynamics in fundamental processes such as cell cycle, intracellular transport, and cell motility, but how +TIPs are regulated during mitosis remains largely unclear. Here we show that the endogenous end-binding protein family EB3 is stable during mitosis, facilitates cell cycle progression at prometaphase, and then is down-regulated during the transition to G(1) phase. The ubiquitin-protein isopeptide ligase SIAH-1 facilitates EB3 polyubiquitination and subsequent proteasome-mediated degradation, whereas SIAH-1 knockdown increases EB3 stability and steady-state levels. Two mitotic kinases, Aurora-A and Aurora-B, phosphorylate endogenous EB3 at Ser-176, and the phosphorylation triggers disruption of the EB3-SIAH-1 complex, resulting in EB3 stabilization during mitosis. Our results provide new insight into a regulatory mechanism of +TIPs in cell cycle transition.

Indexed as

Amino Acid SequenceAnimalsAurora Kinase BAurora KinasesChlorocebus aethiopsCOS CellsHeLa CellsHumansIsoenzymesMicrotubule-Associated ProteinsMicrotubulesMitosisMolecular Sequence DataNuclear ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsAURKB protein, humanAurora Kinase BAurora KinasesIsoenzymesMAPRE3 protein, humanMicrotubule-Associated ProteinsNuclear ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRNA, Small InterferingSeven in Absentia ProteinsUbiquitin-Protein Ligases

Identifiers

PMID19696028
PMCPMC2788886
OpenAlexW2035773876

What OpenQuestion holds

Textmetadata
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.