Evidence map›Paper›PMID 15534215›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Activation of Arp2/3 complex-dependent actin polymerization by plant proteins distantly related to Scar/WAVE.

Mary Frank, Coumaran Egile, Julia Dyachok, Stevan Djakovic, Michelle Nolasco, Rong Li, Laurie G Smith

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed, 77 citations in OpenAlex.

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  6. The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  14. ARP2/3-independent WAVE/SCAR pathway and class XI myosin control sperm nuclear migration in flowering plants.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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.

Mary FrankSection of Cell and Developmental Biology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0116, USA.
Coumaran Egile
Julia Dyachok
Stevan Djakovic
Michelle Nolasco
Rong Li
Laurie G Smith
Harvard University · USUniversity of California, San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arp2/3 complex, a highly conserved nucleator of F-actin polymerization, plays a key role in the regulation of actin dynamics eukaryotic cells. In animal cells and yeasts, Wiskott-Aldrich Syndrome protein (WASP)/suppressor of cAMP receptor (Scar)/WASP family verprolin homologous (WAVE) family proteins activate the Arp2/3 complex in response to localized cues. Like other eukaryotes, plants have an Arp2/3 complex, which has recently been shown to play an important role in F-actin organization and cell morphogenesis. However, no activators of the Arp2/3 complex have been identified in plants, which lack obvious homologs of WASP/Scar/WAVE family proteins. Here, we identify a family of Scar/WAVE-related plant Arp2/3 activators. Like Scar/WAVE proteins, four proteins identified in Arabidopsis thaliana (AtSCAR1 to AtSCAR4) and one in maize (ZmSCAR1) have a C-terminal WASP homology 2 (WH2)/acidic (WA)-verprolin homology/cofilin homology/acidic (VCA)-like domain, which we show can activate the bovine Arp2/3 complex. At their N termini, AtSCAR1 to ATSCAR4, along with a fifth protein lacking a VCA/WA-like domain at its C terminus (At4g18600), are related to the N-terminal Scar homology domains of Scar/WAVE family proteins. Analysis of gene expression patterns suggests functional redundancy among members of the AtSCAR family. Full-length AtSCAR1 and ATSCAR3 proteins and their Scar homology domains bind in vitro to AtBRICK 1 (AtBRK1), the Arabidopsis homolog of HSPC300, a WAVE-binding protein recently identified as a component of a complex implicated in the regulation of Scar/WAVE activity. Thus, AtSCAR proteins are likely to function in association with AtBRK1, and perhaps other Arabidopsis homologs of WAVE complex components, to regulate activation of the Arp2,3 complex in vivo.

Indexed as

Actin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3ActinsAmino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsBase SequenceDNA, PlantGenes, PlantMicrofilament ProteinsMolecular Sequence DataMultiprotein ComplexesPlant ProteinsRecombinant Fusion ProteinsActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3ActinsArabidopsis ProteinsARP2 protein, ArabidopsisBRK1 protein, ArabidopsisDIS1 protein, ArabidopsisDNA, PlantMicrofilament ProteinsMultiprotein ComplexesPlant ProteinsRecombinant Fusion ProteinsWiskott-Aldrich Syndrome Protein Family

Identifiers

PMID15534215
PMCPMC528980
OpenAlexW2142039636

What OpenQuestion holds

Textmetadata
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.