Evidence map›Paper›PMID 28407416›Full record

ArticleCytoskeleton (Hoboken, N.J.)2017

Tau-based fluorescent protein fusions to visualize microtubules.

Paul Mooney, Taylor Sulerud, James F Pelletier, Matthew R Dilsaver, Miroslav Tomschik, Christoph Geisler, Jesse C Gatlin

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2017. 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
1.5field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 21 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

7 authors at 2 institutions in 1 country.

Paul MooneyDepartment of Molecular Biology, University of Wyoming, Laramie, Wyoming, 82071, USA.ORCID http://orcid.org/0000-0003-1997-1686
Taylor SulerudDepartment of Molecular Biology, University of Wyoming, Laramie, Wyoming, 82071, USA.
James F PelletierCell Organization and Division Group, Marine Biological Laboratories, Woods Hole, Massachusetts, 02543, USA.
Matthew R DilsaverDepartment of Molecular Biology, University of Wyoming, Laramie, Wyoming, 82071, USA.
Miroslav TomschikDepartment of Molecular Biology, University of Wyoming, Laramie, Wyoming, 82071, USA.
Christoph GeislerGlycoBac, LLC, Laramie, Wyoming, 82072, USA.
Jesse C GatlinDepartment of Molecular Biology, University of Wyoming, Laramie, Wyoming, 82071, USA.
University of Wyoming · USMarine Biological Laboratory · US

Funding

Wyoming INBRE Phase 4- Equipment Supplement for x-ray diffractometer for Center for Advanced Scientific InstrumentationP20GM103432 · NIGMS · UNIVERSITY OF WYOMING · PI Nicolas A. Blouin · 2012 to 2026
$56.8M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR01GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1988 to 2018
$6.2M
Mechanics of Bipolar Mitotic Spindle AssemblyR01GM102428 · NIGMS · UNIVERSITY OF WYOMING · PI GATLIN, JESSE C · 2012 to 2016
$1.3M
Mechanisms of Steady-State Nuclear Size Regulation in XenopusR15GM106318 · NIGMS · UNIVERSITY OF WYOMING · PI LEVY, DANIEL LEON · 2013 to 2013
$311k
NIGMS NIH HHS P20 GM103432NIGMS NIH HHS R01 GM039565NIGMS NIH HHS R01 GM102428NIGMS NIH HHS R15 GM106318
6 · The paper itself

Abstract

The ability to visualize cytoskeletal proteins and their dynamics in living cells has been critically important in advancing our understanding of numerous cellular processes, including actin- and microtubule (MT)-dependent phenomena such as cell motility, cell division, and mitosis. Here, we describe a novel set of fluorescent protein (FP) fusions designed specifically to visualize MTs in living systems using fluorescence microscopy. Each fusion contains a FP module linked in frame to a modified phospho-deficient version of the MT-binding domain of Tau (mTMBD). We found that expressed and purified constructs containing a single mTMBD decorated Xenopus egg extract spindles more homogenously than similar constructs containing the MT-binding domain of Ensconsin, suggesting that the binding affinity of mTMBD is minimally affected by localized signaling gradients generated during mitosis. Furthermore, MT dynamics were not grossly perturbed by the presence of Tau-based FP fusions. Interestingly, the addition of a second mTMBD to the opposite terminus of our construct caused dramatic changes to the spatial localization of probes within spindles. These results support the use of Tau-based FP fusions as minimally perturbing tools to accurately visualize MTs in living systems.

Indexed as

AnimalsLuminescent ProteinsMicroscopy, FluorescenceMicrotubulesProtein DomainsRecombinant Fusion Proteinstau ProteinsXenopus laevisXenopus ProteinsLuminescent ProteinsRecombinant Fusion Proteinstau ProteinsXenopus Proteinsfluorescent proteinmicrotubulemicrotubule-associated proteinmitotic spindleTauXenopus

Identifiers

PMID28407416
PMCPMC5592782
OpenAlexW2606338817

What OpenQuestion holds

Textmetadata
LicenceTDM
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.