Evidence map›Paper›PMID 24706950›Full record

ArticleJournal of cell science2014

GAS2-like proteins mediate communication between microtubules and actin through interactions with end-binding proteins.

Matthew J Stroud, Alicja Nazgiewicz, Edward A McKenzie, Yisu Wang, Richard A Kammerer, Christoph Ballestrem

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

47 citing papers in PubMed, 63 citations in OpenAlex.

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  15. Microtubules in insulin action: what's on the tube?Trends in endocrinology and metabolism: TEM · 2021
    Review
  16. Article
  17. Article
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  19. Motile cilia genetics and cell biology: big results from little mice.Cellular and molecular life sciences : CMLS · 2021
    Review
  20. 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

6 authors at 2 institutions in 2 countries.

Matthew J StroudWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
Alicja NazgiewiczWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
Edward A McKenzieManchester Institute of Biotechnology, Faculty of Life Sciences, 131 Princess Street, Manchester M1 7DN, UK.
Yisu WangWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
Richard A KammererLaboratory of Biomolecular Research, OFLC 106, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
Christoph BallestremWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK christoph.ballestrem@manchester.ac.uk.
University of Manchester · GBPaul Scherrer Institute · CH

Funding

Biotechnology and Biological Sciences Research Council BB/G004552Biotechnology and Biological Sciences Research Council BB/G004552/1Wellcome Trust
6 · The paper itself

Abstract

Crosstalk between the microtubule (MT) and actin cytoskeletons is fundamental to many cellular processes including cell polarisation and cell motility. Previous work has shown that members of the growth-arrest-specific 2 (GAS2) family mediate the crosstalk between filamentous actin (F-actin) and MTs, but the molecular basis of this process remained unclear. By using fluorescence microscopy, we demonstrate that three members of this family, GAS2-like 1, GAS2-like 2 and GAS2-like 3 (G2L1, G2L2 and G2L3, also known as GAS2L1, GAS2L2 and GAS2L3, respectively) are differentially involved in mediating the crosstalk between F-actin and MTs. Although all localise to actin and MTs, only the exogenous expression of G2L1 and G2L2 influenced MT stability, dynamics and guidance along actin stress fibres. Biochemical analysis and live-cell imaging revealed that their functions are largely due to the association of these proteins with MT plus-end-binding proteins that bind to SxIP or SxLP motifs located at G2L C-termini. Our findings lead to a model in which end-binding (EB) proteins play a key role in mediating actin-MT crosstalk.

Indexed as

ActinsAnimalsCell Line, TumorChlorocebus aethiopsCHO CellsConserved SequenceCOS CellsCricetinaeCricetulusHumansMiceMicrofilament ProteinsMicrotubule-Associated ProteinsMicrotubulesNIH 3T3 CellsProtein BindingActinsGAS2L1 protein, humanGAS2L2 protein, humanMAPRE1 protein, humanMicrofilament ProteinsMicrotubule-Associated ProteinsProtein Sorting SignalsActinEnd-binding proteinGAS2 familyGAS2-like 1GAS2-like 2GAS2-like 3MicrotubuleMtLSMT-tip localising signal

Identifiers

PMID24706950
PMCPMC4058111
OpenAlexW2162868252

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.