Evidence map›Paper›PMID 23223240›Full record

ArticleThe Journal of biological chemistry2013

Phosphorylation of actin-related protein 2 (Arp2) is required for normal development and cAMP chemotaxis in Dictyostelium.

Chang-Hoon Choi, Peter A Thomason, Mehreen Zaki, Robert H Insall, Diane L Barber

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Diverse Family of Arp2/3 Complexes.Trends in cell biology · 2017
    Review
  5. Review
  6. Article
  7. Article
  8. Article
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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

5 authors at 3 institutions in 2 countries.

Chang-Hoon ChoiDepartment of Cell and Tissue Biology, University of California, San Francisco, California 94143, USA.
Peter A Thomason
Mehreen Zaki
Robert H Insall
Diane L Barber
Cancer Research UK Scotland Institute · GBCell and Tissue Systems (United States) · USUniversity of California, San Francisco · US

Funding

Actions of the Sodium-Hydrogen Exchanger Subtype, NHE1R01GM058642 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BARBER, DIANE L · 1999 to 2012
$3.4M
PROGRAM IN CRANIOFACIAL &SKELETAL BIOC06RR016490 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BERTOLAMI, CHARLES N · 2001 to 2001
$2.0M
Preventing hair cell loss by regulating prestin's functionRC1DC010633 · NIDCD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ZHENG, JING · 2009 to 2010
$953k
Cancer Research UK 15672Medical Research Council G117/537NCRR NIH HHS C06 RR016490NCRR NIH HHS C06 RR16490NIDCD NIH HHS DC010633NIGMS NIH HHS R01 GM058642
6 · The paper itself

Abstract

Phosphorylation of the actin-related protein 2 (Arp2) subunit of the Arp2/3 complex on evolutionarily conserved threonine and tyrosine residues was recently identified and shown to be necessary for nucleating activity of the Arp2/3 complex and membrane protrusion of Drosophila cells. Here we use the Dictyostelium diploid system to replace the essential Arp2 protein with mutants that cannot be phosphorylated at Thr-235/6 and Tyr-200. We found that aggregation of the resulting mutant cells after starvation was substantially slowed with delayed early developmental gene expression and that chemotaxis toward a cAMP gradient was defective with loss of polarity and attenuated F-actin assembly. Chemotaxis toward cAMP was also diminished with reduced cell speed and directionality and shorter pseudopod lifetime when Arp2 phosphorylation mutant cells were allowed to develop longer to a responsive state similar to that of wild-type cells. However, clathrin-mediated endocytosis and chemotaxis under agar to folate in vegetative cells were only subtly affected in Arp2 phosphorylation mutants. Thus, phosphorylation of threonine and tyrosine is important for a subset of the functions of the Arp2/3 complex, in particular an unexpected major role in regulating development.

Indexed as

Actin CytoskeletonActin-Related Protein 2ActinsAllelesAnimalsCell MovementChemotaxisCyclic AMPDictyosteliumEndocytosisModels, BiologicalMutationPhosphorylationSpectroscopy, Fourier Transform InfraredTyrosineActin-Related Protein 2ActinsCyclic AMPTyrosine

Identifiers

PMID23223240
PMCPMC3554915
OpenAlexW1976716342

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.