Evidence map›Paper›PMID 27911716›Full record

ReviewBiochemical Society transactions2016

WASP family proteins, more than Arp2/3 activators.

Joe J Tyler, Ellen G Allwood, Kathryn R Ayscough

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

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  20. Disruption of Thrombocyte and T Lymphocyte Development by a Mutation inJournal of immunology (Baltimore, Md. : 1950) · 2017
    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

3 authors at 1 institution in 1 country.

Joe J TylerDepartment of Biomedical Science, Firth Court, University of Sheffield, Sheffield S10 2TN, U.K.
Ellen G AllwoodDepartment of Biomedical Science, Firth Court, University of Sheffield, Sheffield S10 2TN, U.K.
Kathryn R AyscoughDepartment of Biomedical Science, Firth Court, University of Sheffield, Sheffield S10 2TN, U.K.
University of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J014443/1Biotechnology and Biological Sciences Research Council BB/N007581/1
6 · The paper itself

Abstract

Wiskott-Aldrich syndrome protein (WASP) family proteins have been extensively characterized as factors that promote the nucleation of actin through the activation of the protein complex Arp2/3. While yeast mostly have a single member of the family, mammalian cells have at least six different members, often with multiple isoforms. Members of the family are characterized by a common structure. Their N-termini are varied and are considered to confer spatial and temporal regulation of Arp2/3-activating activity, whereas their C-terminal half contains a polyproline-rich region, one or more WASP homology-2 (WH2) actin-binding domains and motifs that bind directly to Arp2/3. Recent studies, however, indicate that the yeast WASP homologue Las17 is able to nucleate actin independently of Arp2/3 through the function of novel G-actin-binding activities in its polyproline region. This allows Las17 to generate the mother filaments that are needed for subsequent Arp2/3 recruitment and activation during the actin polymerization that drives endocytic invagination in yeast. In this review, we consider how motifs within the polyproline region of Las17 support nucleation of actin filaments, and whether similar mechanisms might exist among other family members.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexAnimalsHumansModels, BiologicalPeptidesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsWiskott-Aldrich Syndrome ProteinActin-Related Protein 2-3 ComplexLAS17 protein, S cerevisiaePeptidespolyprolineSaccharomyces cerevisiae ProteinsWiskott-Aldrich Syndrome ProteinactinArp2/3Las17nucleationpolyprolineWH2

Identifiers

PMID27911716
PMCPMC5095904
OpenAlexW2532726012

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.