Evidence map›Paper›PMID 26585311›Full record

ArticleJournal of cell science2016

The Gas2 family protein Pigs is a microtubule +TIP that affects cytoskeleton organisation.

Gemma C Girdler, Derek A Applewhite, Wick M G Perry, Stephen L Rogers, Katja Röper

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Actin-microtubule crosstalk in cell biology.Nature reviews. Molecular cell biology · 2019
    Review
  5. Article
  6. Katja Röper: Deciphering tissue origami.The Journal of cell biology · 2016
    Article
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

5 authors at 3 institutions in 2 countries.

Gemma C GirdlerMRC-Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Derek A ApplewhiteDepartment of Biology & Carolina Center for Genome Sciences, The University of North Carolina at Chapel Hill, Campus Box 3280, 422 Fordham Hall, Chapel Hill, NC 27599-3280, USA Department of Biology, Reed College, 3203 SE Woodstock Boulevard, Portland, OR 97202, USA.
Wick M G PerryDepartment of Biology, Reed College, 3203 SE Woodstock Boulevard, Portland, OR 97202, USA.
Stephen L RogersDepartment of Biology & Carolina Center for Genome Sciences, The University of North Carolina at Chapel Hill, Campus Box 3280, 422 Fordham Hall, Chapel Hill, NC 27599-3280, USA SRogers@bio.unc.edu kroeper@mrc-lmb.cam.ac.uk.
Katja RöperMRC-Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK SRogers@bio.unc.edu kroeper@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GBUniversity of North Carolina at Chapel Hill · USReed College · US

Funding

The Role of the Spectraplakin Short-Stop in Cell MigrationK01CA163972 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI APPLEWHITE, DEREK ANTHONY · 2012 to 2014
$262k
Single molecule analysis of cytoskeletal cross-linking proteinsR03MH101647 · NIMH · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN · 2013 to 2014
$152k
Medical Research Council MC_U105178780Medical Research Council MC_UP_1201/11Medical Research Council U105178780NCI NIH HHS K01 CA163972NCI NIH HHS K01-CA163972-01NIMH NIH HHS 5R03MH101647NIMH NIH HHS R03 MH101647Wellcome TrustWellcome Trust WT090279MA
6 · The paper itself

Abstract

Coordination between different cytoskeletal systems is crucial for many cell biological functions, including cell migration and mitosis, and also plays an important role during tissue morphogenesis. Proteins of the class of cytoskeletal crosslinkers, or cytolinkers, have the ability to interact with more than one cytoskeletal system at a time and are prime candidates to mediate any coordination. One such class comprises the Gas2-like proteins, combining a conserved calponin-homology-type actin-binding domain and a Gas2 domain predicted to bind microtubules (MTs). This domain combination is also found in spectraplakins, huge cytolinkers that play important roles in many tissues in both invertebrates and vertebrates. Here, we dissect the ability of the single Drosophila Gas2-like protein Pigs to interact with both actin and MT cytoskeletons, both in vitro and in vivo, and illustrate complex regulatory interactions that determine the localisation of Pigs to and its effects on the cytoskeleton.

Indexed as

Cell PolarityActin CytoskeletonActinsAmino Acid MotifsAnimalsCells, CulturedDrosophila melanogasterDrosophila ProteinsIntracellular Signaling Peptides and ProteinsMicrotubulesMutationProtein BindingProtein Structure, TertiaryActinsDrosophila ProteinsIntracellular Signaling Peptides and ProteinsPigs protein, DrosophilaActinCytolinkerCytoskeletonDrosophilaGas2-likeMicrotubule

Identifiers

PMID26585311
PMCPMC4732294
OpenAlexW2206499868

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.