Evidence map›Paper›PMID 27872152›Full record

ArticleJournal of cell science2016

An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.

Yuzy Matsuo, Sebastian P Maurer, Masashi Yukawa, Silva Zakian, Martin R Singleton, Thomas Surrey, Takashi Toda

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 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
4.5field-weighted citation impact, top 5% 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, 36 citations in OpenAlex.

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  15. Microtubule dynamics: an interplay of biochemistry and mechanics.Nature reviews. Molecular cell biology · 2018
    Review
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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

7 authors at 4 institutions in 3 countries.

Yuzy MatsuoSynthetic and Systems Biochemistry of the Microtubule Cytoskeleton Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Sebastian P MaurerSynthetic and Systems Biochemistry of the Microtubule Cytoskeleton Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Masashi YukawaHiroshima Research Center for Healthy Aging (HiHA), Department of Molecular Biotechnology, Graduate School of Advanced Science of Matter, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8530, Japan.
Silva ZakianStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Martin R SingletonStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Thomas SurreySynthetic and Systems Biochemistry of the Microtubule Cytoskeleton Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK Thomas.Surrey@crick.ac.uk takashi-toda@hiroshima-u.ac.jp.
Takashi TodaCell Regulation Laboratory, The Francis Crick Institute, 44 Lincoln's Inn Fields, London WC2A 3LY, UK Thomas.Surrey@crick.ac.uk takashi-toda@hiroshima-u.ac.jp.ORCID 0000-0001-7851-1757
The Francis Crick Institute · GBHiroshima University · JPThe Honourable Society of Lincoln's Inn · GBUniversitat Pompeu Fabra · ES

Funding

Cancer Research UK 15656Cancer Research UK 19343Cancer Research UK FC001155Cancer Research UK FC001163Cancer Research UK FC001184Medical Research Council FC001155Medical Research Council FC001163Medical Research Council FC001184Wellcome Trust FC001155Wellcome Trust FC001163Wellcome Trust FC001184
6 · The paper itself

Abstract

Dynamic microtubule plus-ends interact with various intracellular target regions such as the cell cortex and the kinetochore. Two conserved families of microtubule plus-end-tracking proteins, the XMAP215, ch-TOG or CKAP5 family and the end-binding 1 (EB1, also known as MAPRE1) family, play pivotal roles in regulating microtubule dynamics. Here, we study the functional interplay between fission yeast Dis1, a member of the XMAP215/TOG family, and Mal3, an EB1 protein. Using an in vitro microscopy assay, we find that purified Dis1 autonomously tracks growing microtubule ends and is a bona fide microtubule polymerase. Mal3 recruits additional Dis1 to microtubule ends, explaining the synergistic enhancement of microtubule dynamicity by these proteins. A non-canonical binding motif in Dis1 mediates the interaction with Mal3. X-ray crystallography shows that this new motif interacts in an unconventional configuration with the conserved hydrophobic cavity formed within the Mal3 C-terminal region that typically interacts with the canonical SXIP motif. Selectively perturbing the Mal3-Dis1 interaction in living cells demonstrates that it is important for accurate chromosome segregation. Whereas, in some metazoans, the interaction between EB1 and the XMAP215/TOG family members requires an additional binding partner, fission yeast relies on a direct interaction, indicating evolutionary plasticity of this critical interaction module.

Indexed as

Chromosome SegregationAmino AcidsAnimalsBinding SitesCrystallography, X-RayMicrotubule-Associated ProteinsMicrotubulesModels, MolecularProtein BindingProtein DomainsSchizosaccharomycesSchizosaccharomyces pombe ProteinsAmino Acidsdis1 protein, S pombeMal3 protein, S pombeMicrotubule-Associated ProteinsSchizosaccharomyces pombe ProteinsCrystallographyEB1Microtubule polymeraseTIRF microscopyTOGXMAP215

Identifiers

PMID27872152
PMCPMC5201023
OpenAlexW2555384777

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.