Evidence map›Paper›PMID 27528609›Full record

ArticleThe Journal of biological chemistry2016

MICAL3 Flavoprotein Monooxygenase Forms a Complex with Centralspindlin and Regulates Cytokinesis.

Qingyang Liu, Fan Liu, Ka Lou Yu, Roderick Tas, Ilya Grigoriev, Sanne Remmelzwaal, Andrea Serra-Marques, Lukas C Kapitein, Albert J R Heck, Anna Akhmanova

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 33 citations in OpenAlex.

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  10. Membrane and organelle dynamics during cell division.Nature reviews. Molecular cell biology · 2020
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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

10 authors at 1 institution in 1 country.

Qingyang LiuFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Fan Liuthe Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CH Utrecht, The Netherlands.
Ka Lou YuFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Roderick TasFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Ilya GrigorievFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Sanne RemmelzwaalFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Andrea Serra-MarquesFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Lukas C KapiteinFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and.
Albert J R Heckthe Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CH Utrecht, The Netherlands.
Anna AkhmanovaFrom the Cell Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht and a.akhmanova@uu.nl.ORCID 0000-0002-9048-8614
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During cytokinesis, the antiparallel array of microtubules forming the central spindle organizes the midbody, a structure that anchors the ingressed cleavage furrow and guides the assembly of abscission machinery. Here, we identified a role for the flavoprotein monooxygenase MICAL3, an actin disassembly factor, in organizing midbody-associated protein complexes. By combining cell biological assays with cross-linking mass spectrometry, we show that MICAL3 is recruited to the central spindle and the midbody through a direct interaction with the centralspindlin component MKLP1. Knock-out of MICAL3 leads to an increased frequency of cytokinetic failure and a delayed abscission. In a mechanism independent of its enzymatic activity, MICAL3 targets the adaptor protein ELKS and Rab8A-positive vesicles to the midbody, and the depletion of ELKS and Rab8A also leads to cytokinesis defects. We propose that MICAL3 acts as a midbody-associated scaffold for vesicle targeting, which promotes maturation of the intercellular bridge and abscission.

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsCytokinesisGene Knockdown TechniquesHeLa CellsHumansMicrotubule-Associated ProteinsMixed Function OxygenasesNerve Tissue ProteinsPhosphoproteinsrab GTP-Binding ProteinsSpindle ApparatusAdaptor Proteins, Signal TransducingCell Cycle ProteinsERC1 protein, humanMICAL3 protein, humanMicrotubule-Associated ProteinsMixed Function OxygenasesNerve Tissue ProteinsPhosphoproteinsRAB8A protein, humanrab GTP-Binding Proteinsspindlinactincentralspindlincytokinesisflavoprotein monooxygenasemass spectrometry (MS)microtubulemidbodyprotein cross-linkingvesicle transport

Identifiers

PMID27528609
PMCPMC5034054
OpenAlexW2513713807

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.